https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Alice+ClarkProteopedia - User contributions [en]2026-09-12T21:35:46ZUser contributionsMediaWiki 1.43.8https://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3365235Alice Clark/BRCT2021-03-10T14:38:48Z<p>Alice Clark: </p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene='86/868791/Alices_rainbow_selection/1' /><br />
<br />
[[Image:Screenshot_2021-02-25_at_15.36.50.png|350px|right|thumb| MCR1]]<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<scene name='86/868791/Rainbow_veiw/1'>test rainbow</scene><br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3365220Alice Clark/BRCT2021-03-10T14:37:57Z<p>Alice Clark: </p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene='86/868791/Alices_rainbow_selection/1' /><br />
<br />
[Image:Screenshot_2021-02-25_at_15.36.50.png|350px|right|thumb| MCR1]]<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<scene name='86/868791/Rainbow_veiw/1'>test rainbow</scene><br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3364957Alice Clark/BRCT2021-03-10T14:23:12Z<p>Alice Clark: </p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene='86/868791/Alices_rainbow_selection/1' /><br />
<br />
[size='350' [Image:Screenshot_2021-02-25_at_15.36.50.png]]<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<scene name='86/868791/Rainbow_veiw/1'>test rainbow</scene><br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3364943Alice Clark/BRCT2021-03-10T14:22:08Z<p>Alice Clark: </p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene='86/868791/Alices_rainbow_selection/1' /><br />
<br />
[[Image:Screenshot_2021-02-25_at_15.36.50.png]]<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<scene name='86/868791/Rainbow_veiw/1'>test rainbow</scene><br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=File:Screenshot_2021-02-25_at_15.36.50.png&diff=3364888File:Screenshot 2021-02-25 at 15.36.50.png2021-03-10T14:17:48Z<p>Alice Clark: </p>
<hr />
<div>== Licensing ==<br />
{{self|cc-by-sa-3.0|GFDL}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3364858Alice Clark/BRCT2021-03-10T14:11:39Z<p>Alice Clark: </p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene='86/868791/Alices_rainbow_selection/1' /><br />
<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<scene name='86/868791/Rainbow_veiw/1'>test rainbow</scene><br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3364856Alice Clark/BRCT2021-03-10T14:08:31Z<p>Alice Clark: </p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene name='86/868791/Alices_rainbow_selection/1' /><br />
<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<scene name='86/868791/Rainbow_veiw/1'>test rainbow</scene><br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3364854Alice Clark/BRCT2021-03-10T14:03:38Z<p>Alice Clark: </p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene name='86/868791/Rainbow_veiw/1'>test</scene' /><br />
<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<scene name='86/868791/Rainbow_veiw/1'>test rainbow</scene><br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3364852Alice Clark/BRCT2021-03-10T14:02:10Z<p>Alice Clark: Undo revision 3364849 by Alice Clark (Talk)</p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene='<scene name='86/868791/Rainbow_veiw/1'>TextToBeDisplayed</scene>' /><br />
<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<scene name='86/868791/Rainbow_veiw/1'>test rainbow</scene><br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3364850Alice Clark/BRCT2021-03-10T14:00:57Z<p>Alice Clark: Undo revision 3364849 by Alice Clark (Talk)</p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene='<scene name='86/868791/Rainbow_veiw/1'>TextToBeDisplayed</scene>' /><br />
<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3364849Alice Clark/BRCT2021-03-10T14:00:15Z<p>Alice Clark: </p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene='<scene name='86/868791/Rainbow_veiw/1 /><br />
<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3364848Alice Clark/BRCT2021-03-10T13:59:12Z<p>Alice Clark: </p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene='<scene name='86/868791/Rainbow_veiw/1'>TextToBeDisplayed</scene>' /><br />
<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3364846Alice Clark/BRCT2021-03-10T13:40:24Z<p>Alice Clark: </p>
<hr />
<div><Structure load='6w25' size='350' frame='true' align='right' caption='Melanocrtin 4 Receptor' scene='Insert optional scene name here' /><br />
<br />
<br />
==Melanocortin 1 Receptor: An insight to MCR1 structure, function and regulation==<br />
===Introduction to MC1R===<br />
The highly polymorphic human MC1R gene, located on chromosome 16q24.3 encodes for a MCR1 receptor also known as melanocyte -stimulating hormone receptor. The melanocortin receptor family consists of five members: MC1R, MCR2, MCR3, MC4R and MC5R all of which exhibit functions and are expressed differently (Wolf Horrell, Boulanger and D’Orazio, 2016). The gene is expressed in melanocytes along with other cell types that inhabit the skin such as keratinocytes and fibroblast as well as cells that operate the immune system (Gruis and Doorn, 2012). The activation of the MC1R receptor by ultraviolet radiation increases the production of the dark eumelanin pigment, resulting in the darkening of the skin. MCR1 stimulation also results in increased melanocyte dendricity, proliferation, cell survival and DNA repair. The loss of melanocortin receptor function results in the production of the red/yellow pheomelanin pigment by melanocytes, resulting in the red hair, fair skin, poor tanning, freckling and increased skin cancer risk in humans (Beaumont et al., 2011). <br />
===Determination of MC1R Structure===<br />
The mature MC1R protein is made up of 317 amino acids and a 7 a-helical transmembrane domain. Based on the sequence similarity analysis, the melanocortin receptor family belong to the class A of G-coupled protein receptors therefore direct information on their secondary and tertiary structures is limited as G coupled protein receptors are resistant to crystallisation (Garcia-Borron, Sanchez-Laorden and Jimenez-Cervantes, 2005) (Zhao and Wu, 2012). <br />
<br />
MC4R<br />
Ligands<br />
<br />
<br />
<br />
<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene><br />
<scene name='pdbligand=4J2:(2R)-2-AMINO-3-(NAPHTHALEN-2-YL)PROPANOIC+ACID'>4J2</scene><br />
<br />
<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3323092Alice Clark/BRCT2020-11-25T15:29:34Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<scene name='86/868791/Hennas_protein/1'>hot pink protein</scene><br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3323091Alice Clark/BRCT2020-11-25T15:21:14Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<scene name='86/868791/Hennas_protein/1'>hot pink protein</scene><br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
The F1 and Axle<br />
<br />
The <scene name='86/868791/Alices_1t15/2'>BRCA Protein</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
---<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar moiety and the base moiety. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is removed from the rotor by an <scene name='78/781973/Arg/1'>arginine</scene> amino acid, into a charged pocket, and then is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region. How many Transmembrane α-helices are there?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that influence the hydrogen ions's path within the the F0. Which one acts like a broom sweeping the protons off the rotor?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = Adenosine triphosphate (nucleotide)<br />
<br />
ADP = Adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = An acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = An acidic amino acid (negatively charged)<br />
<br />
Arginine = A basic amino acid (positively charged)<br />
<br />
Transmembrane α-helices = Membrane-spanning α-helices<br />
<br />
ATP synthase = A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
Moiety = A "part" or "functional group" of a molecule<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3323087Alice Clark/BRCT2020-11-25T14:49:24Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
The F1 and Axle<br />
<br />
The <scene name='86/868791/Alices_1t15/2'>BRCA Protein</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
---<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar moiety and the base moiety. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is removed from the rotor by an <scene name='78/781973/Arg/1'>arginine</scene> amino acid, into a charged pocket, and then is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region. How many Transmembrane α-helices are there?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that influence the hydrogen ions's path within the the F0. Which one acts like a broom sweeping the protons off the rotor?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = Adenosine triphosphate (nucleotide)<br />
<br />
ADP = Adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = An acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = An acidic amino acid (negatively charged)<br />
<br />
Arginine = A basic amino acid (positively charged)<br />
<br />
Transmembrane α-helices = Membrane-spanning α-helices<br />
<br />
ATP synthase = A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
Moiety = A "part" or "functional group" of a molecule<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3323086Alice Clark/BRCT2020-11-25T14:47:36Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
The F1 and Axle<br />
<br />
The <scene name='86/868791/Alices_1t15/2'>BRCA Protein</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar moiety and the base moiety. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is removed from the rotor by an <scene name='78/781973/Arg/1'>arginine</scene> amino acid, into a charged pocket, and then is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region. How many Transmembrane α-helices are there?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that influence the hydrogen ions's path within the the F0. Which one acts like a broom sweeping the protons off the rotor?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = Adenosine triphosphate (nucleotide)<br />
<br />
ADP = Adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = An acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = An acidic amino acid (negatively charged)<br />
<br />
Arginine = A basic amino acid (positively charged)<br />
<br />
Transmembrane α-helices = Membrane-spanning α-helices<br />
<br />
ATP synthase = A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
Moiety = A "part" or "functional group" of a molecule<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3323085Alice Clark/BRCT2020-11-25T14:46:29Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='86/868791/Alices_1t15/2'>BRCA Protein</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar moiety and the base moiety. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is removed from the rotor by an <scene name='78/781973/Arg/1'>arginine</scene> amino acid, into a charged pocket, and then is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region. How many Transmembrane α-helices are there?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that influence the hydrogen ions's path within the the F0. Which one acts like a broom sweeping the protons off the rotor?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = Adenosine triphosphate (nucleotide)<br />
<br />
ADP = Adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = An acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = An acidic amino acid (negatively charged)<br />
<br />
Arginine = A basic amino acid (positively charged)<br />
<br />
Transmembrane α-helices = Membrane-spanning α-helices<br />
<br />
ATP synthase = A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
Moiety = A "part" or "functional group" of a molecule<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3323084Alice Clark/BRCT2020-11-25T14:44:26Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='86/868791/Alices_1t15/2'>hello students</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar moiety and the base moiety. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is removed from the rotor by an <scene name='78/781973/Arg/1'>arginine</scene> amino acid, into a charged pocket, and then is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region. How many Transmembrane α-helices are there?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that influence the hydrogen ions's path within the the F0. Which one acts like a broom sweeping the protons off the rotor?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = Adenosine triphosphate (nucleotide)<br />
<br />
ADP = Adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = An acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = An acidic amino acid (negatively charged)<br />
<br />
Arginine = A basic amino acid (positively charged)<br />
<br />
Transmembrane α-helices = Membrane-spanning α-helices<br />
<br />
ATP synthase = A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
Moiety = A "part" or "functional group" of a molecule<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3323083Alice Clark/BRCT2020-11-25T14:30:30Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar moiety and the base moiety. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is removed from the rotor by an <scene name='78/781973/Arg/1'>arginine</scene> amino acid, into a charged pocket, and then is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region. How many Transmembrane α-helices are there?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that influence the hydrogen ions's path within the the F0. Which one acts like a broom sweeping the protons off the rotor?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = Adenosine triphosphate (nucleotide)<br />
<br />
ADP = Adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = An acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = An acidic amino acid (negatively charged)<br />
<br />
Arginine = A basic amino acid (positively charged)<br />
<br />
Transmembrane α-helices = Membrane-spanning α-helices<br />
<br />
ATP synthase = A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
Moiety = A "part" or "functional group" of a molecule<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/BRCT&diff=3323082Alice Clark/BRCT2020-11-25T14:29:52Z<p>Alice Clark: New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...</p>
<hr />
<div>==Your Heading Here (maybe something like 'Structure')==<br />
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Alice Clark/BRCT'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function ==<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875741Alice Clark/ATPsynthase2018-03-24T18:30:39Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar moiety and the base moiety. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is removed from the rotor by an <scene name='78/781973/Arg/1'>arginine</scene> amino acid, into a charged pocket, and then is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region. How many Transmembrane α-helices are there?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that influence the hydrogen ions's path within the the F0. Which one acts like a broom sweeping the protons off the rotor?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = Adenosine triphosphate (nucleotide)<br />
<br />
ADP = Adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = An acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = An acidic amino acid (negatively charged)<br />
<br />
Arginine = A basic amino acid (positively charged)<br />
<br />
Transmembrane α-helices = Membrane-spanning α-helices<br />
<br />
ATP synthase = A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
Moiety = A "part" or "functional group" of a molecule<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875740Alice Clark/ATPsynthase2018-03-24T18:24:35Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar moiety and the base moiety. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is removed from the rotor by an <scene name='78/781973/Arg/1'>arginine</scene> amino acid, into a charged pocket, and then is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region. How many Transmembrane α-helices are there?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that influences the hydrogen ions's path within the the F0?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = Adenosine triphosphate (nucleotide)<br />
<br />
ADP = Adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = An acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = An acidic amino acid (negatively charged)<br />
<br />
Arginine = A basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = Membrane-spanning α-helices<br />
<br />
ATP synthase = A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
Moiety = A "part" or "functional group" of a molecule<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875738Alice Clark/ATPsynthase2018-03-24T10:00:38Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar moiety and the base moiety. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = Adenosine triphosphate (nucleotide)<br />
<br />
ADP = Adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = An acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = An acidic amino acid (negatively charged)<br />
<br />
Arginine = A basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = Membrane-spanning α-helices<br />
<br />
ATP synthase = A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
Moiety = a part or functional group of a molecule<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875695Alice Clark/ATPsynthase2018-03-23T11:39:46Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar group and the base component. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = Adenosine triphosphate (nucleotide)<br />
<br />
ADP = Adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = An acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = An acidic amino acid (negatively charged)<br />
<br />
Arginine = A basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = Membrane-spanning α-helices<br />
<br />
ATP synthase = A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875694Alice Clark/ATPsynthase2018-03-23T11:30:39Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar group and the base component. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = adenosine triphosphate (nucleotide)<br />
<br />
ADP = adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = an acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = an acidic amino acid (negatively charged)<br />
<br />
Arginine = a basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = membrane-spanning α-helices<br />
<br />
ATP synthase - A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875693Alice Clark/ATPsynthase2018-03-23T11:28:45Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, which is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar group and the base component. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = adenosine triphosphate (nucleotide)<br />
<br />
ADP = adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = an acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = an acidic amino acid (negatively charged)<br />
<br />
Arginine = a basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = membrane-spanning α-helices<br />
<br />
ATP synthase - A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875692Alice Clark/ATPsynthase2018-03-23T11:20:42Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right ==> <br />
<br />
It is depicted in 3D with each protein shown in a different colour.<br />
<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, which is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar group and the base component. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = adenosine triphosphate (nucleotide)<br />
<br />
ADP = adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = an acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = an acidic amino acid (negatively charged)<br />
<br />
Arginine = a basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = membrane-spanning α-helices<br />
<br />
ATP synthase - A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875690Alice Clark/ATPsynthase2018-03-23T07:56:18Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown in a different colour.<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, which is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar group and the base component. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the F0 region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = adenosine triphosphate (nucleotide)<br />
<br />
ADP = adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = an acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = an acidic amino acid (negatively charged)<br />
<br />
Arginine = a basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = membrane-spanning α-helices<br />
<br />
ATP synthase - A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875689Alice Clark/ATPsynthase2018-03-23T07:55:01Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown in a different colour.<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, which is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar group and the base component. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region'''<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = adenosine triphosphate (nucleotide)<br />
<br />
ADP = adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = an acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = an acidic amino acid (negatively charged)<br />
<br />
Arginine = a basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = membrane-spanning α-helices<br />
<br />
ATP synthase - A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875688Alice Clark/ATPsynthase2018-03-23T07:53:43Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown in a different colour.<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F1 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, which is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar group and the base component. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region"<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = adenosine triphosphate (nucleotide)<br />
<br />
ADP = adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = an acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = an acidic amino acid (negatively charged)<br />
<br />
Arginine = a basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = membrane-spanning α-helices<br />
<br />
ATP synthase - A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875687Alice Clark/ATPsynthase2018-03-23T07:52:45Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown in a different colour.<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F0 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, which is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar group and the base component. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region"<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = adenosine triphosphate (nucleotide)<br />
<br />
ADP = adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = an acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = an acidic amino acid (negatively charged)<br />
<br />
Arginine = a basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = membrane-spanning α-helices<br />
<br />
ATP synthase - A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875686Alice Clark/ATPsynthase2018-03-23T07:51:33Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown in a different colour.<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F0 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, which is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar group and the base component. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region"<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = adenosine triphosphate (nucleotide)<br />
<br />
ADP = adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = an acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = an acidic amino acid (negatively charged)<br />
<br />
Arginine = a basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = membrane-spanning α-helices<br />
<br />
ATP synthase - A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875685Alice Clark/ATPsynthase2018-03-23T07:48:05Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown in a different colour.<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
<br />
'''The F0 and Axle'''<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, which is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, as the ADP and phosphate binds, the high energy bond is formed and the ATP is released. <br />
<br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
----<br />
'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''<br />
<br />
----<br />
<br />
<br />
'''ADP and ATP are bound in the nucleotide binding sites'''<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar group and the base component. ==><br />
<br />
The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
<br />
----<br />
'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''<br />
<br />
----<br />
<br />
<br />
'''The F0 region"<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = adenosine triphosphate (nucleotide)<br />
<br />
ADP = adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = an acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = an acidic amino acid (negatively charged)<br />
<br />
Arginine = a basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = membrane-spanning α-helices<br />
<br />
ATP synthase - A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875674Alice Clark/ATPsynthase2018-03-22T19:22:26Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown in a different colour.<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains α (alpha) (shown in light blue) and β (beta) (shown in dark blue), and making up the axel, the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
<br />
<br />
The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar and base. ==><br />
<br />
The three sites primarily located in the β subunits carry active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly, they are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
<br />
----<br />
'''Q2: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q3: Between which atoms is the high energy bond formed, within the ATP (the bond that the ATP synthase catalyses within the β subunits)?'''<br />
<br />
----<br />
<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates at 120° steps, putting the motor head into three different conformations, as the ADP and phosphate binds, the high energy bond is formed and the ATP is released. <br />
<br />
----<br />
'''Q4: What is the role of the axel, explain how it acts on the β subunits?'''<br />
<br />
---- <br />
<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices that sit in the mitochondrial membrane. The hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices, of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acid charge. Secondly, after a full rotation, the hydrogen is transferred to an <scene name='78/781973/Arg/1'>arginine</scene> amino acid and is passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen ions's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and phosphate to the ATP synthase beta domain located in the F1 domain<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate using energy, generated by the hydrogen ions moving the F0, then the movement is transmitted by the axel to the F1 region.<br />
<br />
3. Releasing the newly made ATP from the F1 region<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
ATP = adenosine triphosphate (nucleotide)<br />
<br />
ADP = adenosine diphosphate (nucleotide)<br />
<br />
Aspartic acid = an acidic amino acid (negatively charged)<br />
<br />
Glutamic acid = an acidic amino acid (negatively charged)<br />
<br />
Arginine = a basic amino acid (negatively charged)<br />
<br />
Transmembrane α-helices = membrane-spanning α-helices<br />
<br />
ATP synthase - A molecular motor that generates ATP<br />
<br />
Hydrogen ion = A hydrogen ion is created when a hydrogen atom loses or gains an electron. A positively charged hydrogen ion is also referred to as a proton<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2875668Alice Clark/ATPsynthase2018-03-22T18:32:59Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown in a different colour.<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains alpha (shown in light blue) and beta (shown in dark blue), and making up the axel, the <scene name='78/781973/Gamma/1'>gamma</scene> protein chain. <br />
<br />
----<br />
'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''<br />
<br />
----<br />
<br />
<br />
The F1 can have adenosine diphosphate (ADP) molecules and adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene> in the nucleotide binding sites. See if you can zoom in on the ATP identify the phosphate atoms (orange). ==><br />
<br />
The three sites primarily located in the β subunits carry active ATP synthesis. The sites primarily located in the α subunits are non-catalytic and exchange bound nucleotide very slowly, they are thought to be a carry over from evolution, and now play a more regulatory role.<br />
<br />
<br />
----<br />
'''Q2: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q3: Which atoms is the high energy bond formed between, within ATP (the bond that the ATP synthase catalyses within the β subunits)?'''<br />
<br />
----<br />
<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates at 120 degree steps, putting the motor into three different conformations, as the ADP and phosphate binds, the high energy bond is formed and the ATP is released. <br />
<br />
----<br />
'''Q4: What is the role of the axel, explain how it effects the β subunits?'''<br />
<br />
---- <br />
<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogen's are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>aspartic acid residues or glutamic acid</scene> (amino acids) in the F0 motor, and then transferred to an <scene name='78/781973/Arg/1'>arginine</scene> (Arg) amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen's within the the F0, during the ATP generation process?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and phosphate to the ATP synthase beta domain located in the F1 domain<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate using energy, generated by the hydrogens moving the F0, then the movement is transmitted by the axel to the F1 region.<br />
<br />
3. Releasing the newly made ATP from the F1 region<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
Aspartic acid = an acidic amino acid <br />
<br />
Glutamic acid = an acidic amino acid<br />
<br />
ATP = adenosine triphosphate (nucleotide)<br />
<br />
ADP = adenosine diphosphate (nucleotide)<br />
<br />
ATP synthase - A molecular motor that generates ATP<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869991Alice Clark/ATPsynthase2018-03-10T17:43:28Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour.<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group has an important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. <br />
<br />
----<br />
'''Q1: How many protein chains comprise the F1 region?'''<br />
<br />
----<br />
<br />
<br />
The F1 binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange).<br />
<br />
----<br />
'''Q2: How many phosphates does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q3: Where is the high energy bond that the ATP synthase forms'''<br />
<br />
----<br />
<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
----<br />
'''Q4: What is the role of the axel?'''<br />
<br />
---- <br />
<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>aspartic acid residues or glutamic acid</scene> (amino acids) in the F0 motor, and then transferred to an <scene name='78/781973/Arg/1'>arginine</scene> (Arg) amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase to the F1 domain<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate using energy, generated by the hydrogens moving the F0, then the movement is transmitted by the axel to the F1 region.<br />
<br />
3. Releasing the newly made ATP from the F1 region<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869990Alice Clark/ATPsynthase2018-03-10T17:42:30Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different <scene name='78/781973/Start/1'>colour</scene>.<br />
<br />
Tools for exploring ATP synthase in 3D<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group has an important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. <br />
<br />
----<br />
'''Q1: How many protein chains comprise the F1 region?'''<br />
<br />
----<br />
<br />
<br />
The F1 binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange).<br />
<br />
----<br />
'''Q2: How many phosphates does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q3: Where is the high energy bond that the ATP synthase forms'''<br />
<br />
----<br />
<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
----<br />
'''Q4: What is the role of the axel?'''<br />
<br />
---- <br />
<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>aspartic acid residues or glutamic acid</scene> (amino acids) in the F0 motor, and then transferred to an <scene name='78/781973/Arg/1'>arginine</scene> (Arg) amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase to the F1 domain<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate using energy, generated by the hydrogens moving the F0, then the movement is transmitted by the axel to the F1 region.<br />
<br />
3. Releasing the newly made ATP from the F1 region<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869989Alice Clark/ATPsynthase2018-03-10T17:37:55Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour.<br />
<br />
''Tools for exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group has an important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. <br />
<br />
----<br />
'''Q1: How many protein chains comprise the F1 region?'''<br />
<br />
----<br />
<br />
<br />
The F1 binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange).<br />
<br />
----<br />
'''Q2: How many phosphates does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q3: Where is the high energy bond that the ATP synthase forms'''<br />
<br />
----<br />
<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
----<br />
'''Q4: What is the role of the axel?'''<br />
<br />
---- <br />
<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>aspartic acid residues or glutamic acid</scene> (amino acids) in the F0 motor, and then transferred to an <scene name='78/781973/Arg/1'>arginine</scene> (Arg) amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase to the F1 domain<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate using energy, generated by the hydrogens moving the F0, then the movement is transmitted by the axel to the F1 region.<br />
<br />
3. Releasing the newly made ATP from the F1 region<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869988Alice Clark/ATPsynthase2018-03-10T17:32:46Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour.<br />
<br />
''Tools for exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group has an important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. <br />
<br />
----<br />
'''Q1: How many protein chains comprise the F1 region?'''<br />
<br />
----<br />
<br />
<br />
The F1 binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange).<br />
<br />
----<br />
'''Q2: How many phosphates does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q3: Where is the high energy bond that the ATP synthase forms'''<br />
<br />
----<br />
<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
----<br />
'''Q4: What is the role of the axel?'''<br />
<br />
---- <br />
<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>aspartic acid residues or glutamic acid</scene> (amino acids) in the F0 motor, and then transferred to an <scene name='78/781973/Arg/1'>arginine</scene> (Arg) amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
'''Summary'''<br />
<br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase to the F1 domain<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate using energy, generated by the hydrogens moving the F0, then the movement is transmitted by the axel to the F1 region.<br />
<br />
3. Releasing the newly made ATP from the F1 region<br />
<br />
<br />
<br />
'''Key Terms'''<br />
<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869987Alice Clark/ATPsynthase2018-03-10T17:25:34Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate<br />
<br />
3. Releasing the newly made ATP<br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour. You are viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
<br />
''Tools for exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
- green text - click to load a new 3D scene<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group has an important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. <br />
<br />
----<br />
'''Q1: How many protein chains comprise the F1 region?'''<br />
<br />
----<br />
<br />
<br />
The F1 binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange).<br />
<br />
----<br />
'''Q2: How many phosphates does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q3: Where is the high energy bond that the ATP synthase forms'''<br />
<br />
----<br />
<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
----<br />
'''Q4: What is the role of the axel?'''<br />
<br />
---- <br />
<br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>aspartic acid residues or glutamic acid</scene> (amino acids) in the F0 motor, and then transferred to an <scene name='78/781973/Arg/1'>arginine</scene> (Arg) amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q5: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q6: Name two key amino acids, one acidic and one basic, that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
<br />
'''Key Terms'''<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869986Alice Clark/ATPsynthase2018-03-10T17:16:43Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate<br />
<br />
3. Releasing the newly made ATP<br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour. You are viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
<br />
''Exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group has an important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. <br />
<br />
----<br />
'''Q1: How many protein chains comprise the F1 region?'''<br />
<br />
----<br />
<br />
The F1 binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange).<br />
<br />
----<br />
'''Q4: How many phosphates does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q5: Where is the high energy bond that the ATP synthase forms'''<br />
<br />
----<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
----<br />
'''Q5: What is the role of the axel?'''<br />
<br />
---- <br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>aspartic acid residues or glutamic acid</scene> (amino acids) in the F0 motor, and then transferred to an <scene name='78/781973/Arg/1'>arginine</scene> (Arg) amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q3: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q4: Name two key amino acids, one acidic and one basic, that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
<br />
'''Key Terms'''<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869985Alice Clark/ATPsynthase2018-03-10T17:08:34Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate<br />
<br />
3. Releasing the newly made ATP<br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour. You are viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
<br />
''Exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group has an important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. <br />
<br />
----<br />
'''Q1: How many protein chains comprise the F1 region?'''<br />
<br />
----<br />
<br />
The F1 binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange).<br />
<br />
<br />
----<br />
'''Q2: How many ATP and ADP can you find and how is related to the number of protein chains in the F1 motor?'''<br />
<br />
----<br />
'''Q4: How many phosphates does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q5: Where is the high energy bond that the ATP synthase forms'''<br />
<br />
----<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
----<br />
'''Q5: What is the role of the axel?'''<br />
<br />
---- <br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>aspartic acid residues or glutamic acid</scene> (amino acids) in the F0 motor, and then transferred to an <scene name='78/781973/Arg/1'>arginine</scene> (ARG) amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q3: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q4: Name two key amino acids, one acidic and one basic, that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
<br />
'''Key Terms'''<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869984Alice Clark/ATPsynthase2018-03-10T17:07:36Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate<br />
<br />
3. Releasing the newly made ATP<br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour. You are viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
<br />
''Exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group has an important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. <br />
<br />
----<br />
'''Q1: How many protein chains comprise the F1 region?'''<br />
<br />
----<br />
<br />
The F1 binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange).<br />
<br />
<br />
----<br />
'''Q2: How many ATP and ADP can you find and how is related to the number of protein chains in the F1 motor?'''<br />
<br />
----<br />
'''Q4: How many phosphates does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q5: Where is the high energy bond that the ATP synthase forms'''<br />
<br />
----<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
----<br />
'''Q5: What is the role of the axel?'''<br />
<br />
---- <br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>''aspartic acid residues''</scene> or glutamic acid (amino acids) in the F0 motor, and then transferred to an <scene name='78/781973/Arg/1'>arginine</scene> (ARG) amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q3: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q4: Name two key amino acids, one acidic and one basic, that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
<br />
'''Key Terms'''<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869983Alice Clark/ATPsynthase2018-03-10T17:06:23Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate<br />
<br />
3. Releasing the newly made ATP<br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour. You are viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
<br />
''Exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group has an important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. <br />
<br />
----<br />
'''Q1: How many protein chains comprise the F1 region?'''<br />
<br />
----<br />
<br />
The F1 binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange).<br />
<br />
<br />
----<br />
'''Q2: How many ATP and ADP can you find and how is related to the number of protein chains in the F1 motor?'''<br />
<br />
----<br />
'''Q4: How many phosphates does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q5: Where is the high energy bond that the ATP synthase forms'''<br />
<br />
----<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
----<br />
'''Q5: What is the role of the axel?'''<br />
<br />
---- <br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>'''aspartic acid residues'''</scene> or glutamic acid (amino acids) in the F0 motor, and then transferred to an <scene name='78/781973/Arg/1'>arginine</scene> (ARG) amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q3: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q4: Name two key amino acids, one acidic and one basic, that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
<br />
'''Key Terms'''<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869982Alice Clark/ATPsynthase2018-03-10T16:43:24Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate<br />
<br />
3. Releasing the newly made ATP<br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour. You are viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
<br />
''Exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group with a important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. It also binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify how many phosphates (atoms shown in orange) are found.<br />
<br />
----<br />
'''Q1: How many chains makeup the F1 region, and what is it's role in generating ATP?'''<br />
<br />
----<br />
'''Q2: How many ATP and ADP can you find and how is related to the number of protein chains in the F1 motor?'''<br />
<br />
----<br />
'''Q4: How many phosphates does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q5: Where is the high energy bond that the ATP synthase forms'''<br />
<br />
----<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>aspartic acid residues</scene> or glutamic acid (amino acids) in the F0 motor, and then transferred to an <scene name='78/781973/Arg/1'>arginine</scene> (ARG) amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q3: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q4: What are the two key amino acid that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
<br />
'''Key Terms'''<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869981Alice Clark/ATPsynthase2018-03-10T16:19:55Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate<br />
<br />
3. Releasing the newly made ATP<br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour. You are viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
<br />
''Exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group with a important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. It also binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify how many phosphates (atoms shown in orange) are found.<br />
<br />
----<br />
'''Q1: How many chains makeup the F1 region, and what is it's role in generating ATP?'''<br />
<br />
----<br />
'''Q2: How many ATP and ADP can you find and how is related to the number of protein chains in the F1 motor?'''<br />
<br />
----<br />
'''Q4: How many phosphates does ATP have, and how does this differ to ADP?'''<br />
<br />
----<br />
'''Q5: Where is the high energy bond that the ATP synthase forms'''<br />
<br />
----<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>aspartic acid residues</scene> or glutamic acid (amino acids) in the F0 motor, and then transferred to an arginine amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q3: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q4: What are the two key amino acid that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
<br />
'''Key Terms'''<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869980Alice Clark/ATPsynthase2018-03-10T15:28:41Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate<br />
<br />
3. Releasing the newly made ATP<br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour. You are viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
<br />
''Exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group with a important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. It also binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify how many phosphates (atoms shown in orange) are found.<br />
<br />
----<br />
'''Q1: How many chains makeup the F1 region, and what is it's role in generating ATP?'''<br />
<br />
----<br />
'''Q2: How many ATP and ADP can you find and how is related to the number of protein chains in the F1 motor?'''<br />
<br />
----<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of <scene name='78/781973/Aspgluchain/1'>aspartic acid residues</scene> (amino acids) in the F0 motor, and then transferred to an arginine amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q3: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q4: What are the two key amino acid that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
ATP synthase is an example of a molecular motor.<br />
<br />
<br />
----<br />
'''Q4: How many phosphates does ATP have?'''<br />
----<br />
'''Q5: How many phosphates does ADP have'''<br />
----<br />
<br />
----<br />
<br />
<br />
Key Terms<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869979Alice Clark/ATPsynthase2018-03-10T15:00:02Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate<br />
<br />
3. Releasing the newly made ATP<br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour. You are viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
<br />
''Exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
<br />
'''Have a go yourself now ==>'''<br />
<br />
<br />
<br />
'''Exploring the ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1, the stator and the axel - each group with a important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. It also binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify how many phosphates (atoms shown in orange) are found.<br />
<br />
----<br />
'''Q1: How many chains makeup the F1 region, and what is it's role in generating ATP?'''<br />
<br />
----<br />
'''Q2: How many ATP and ADP can you find and how is related to the number of protein chains in the F1 motor?'''<br />
<br />
----<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of aspartic acid residues (amino acids) in the F0 motor, and then transferred to an arginine amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
----<br />
'''Q3: What is the location and role of the FO region?'''<br />
<br />
----<br />
'''Q4: What are the two key amino acid that bind the hydrogen's in the ATP generation?'''<br />
<br />
----<br />
<br />
ATP synthase is an example of a molecular motor.<br />
<br />
<br />
----<br />
'''Q4: How many phosphates does ATP have?'''<br />
----<br />
'''Q5: How many phosphates does ADP have'''<br />
----<br />
<br />
----<br />
<br />
<br />
Key Terms<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clarkhttps://proteopedia.org/index.php?title=Alice_Clark/ATPsynthase&diff=2869978Alice Clark/ATPsynthase2018-03-10T14:50:49Z<p>Alice Clark: </p>
<hr />
<div>== '''ATP Synthase''' ==<br />
<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene=''><br />
The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor, found in the mitochondrial membrane, called ATP synthase.<br />
<br />
1. Binding of ADP and the phosphate to ATP synthase<br />
<br />
2. Formation of the new high energy phosphate-phosphate bond between the ADP and phosphate<br />
<br />
3. Releasing the newly made ATP<br />
<br />
ATP synthase is shown here to the right in 3D with each protein shown a different colour, using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].<br />
<br />
<br />
''Exploring ATP synthase in 3D''<br />
<br />
- left mouse button to rotate the protein model.<br />
<br />
- middle mouse button or scroll wheel to zoom (option-click on a Mac)<br />
<br />
- right mouse button for more options and information (control-click on a Mac). <br />
<br />
<br />
''''Have a go yourself now ==>''''<br />
<br />
<br />
<br />
'''The ATP synthase molecule'''<br />
<br />
ATP synthase is built up of different groups of proteins: the F0, the F1 and the axel - each with a important role.<br />
<br />
The <scene name='78/781973/Alpha-beta/1'>F1 motor</scene> contains alpha (shown in light blue) and beta (shown in dark blue) protein chains. It also binds the adenosine diphosphate (ADP) molecules and the adenosine triphosphate (ATP) <scene name='78/781973/Atpandadp/1'>binding sites</scene>. See if you can zoom in on the ATP identify how many phosphates (atoms shown in orange) are found.<br />
<br />
----<br />
'''Q1: Where is the F1 region located within the ATP synthase, and what is its role?'''<br />
<br />
----<br />
'''Q2: How many ATP and ADP can you find and how is related to the number of protein chains in the F1 motor?'''<br />
<br />
----<br />
<br />
The <scene name='78/781973/Axel/1'>axle</scene> rotates putting the motor into three different conformations as the ADP binds, the phosphate bond is formed and the ATP being released. <br />
<br />
<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of alpha helices that sit in the mitochondrial membrane. The hydrogen ions travel around the circular F0 motor, and turning the rotor in the process, much like a water wheel. The hydrogens are passed alone a chain of aspartic acid residues (amino acids) in the F0 motor, and then transferred to an arginine amino acid. The arginine passes the hydrogen to the rotor, which turns all the way around. Then the hydrogen is then passed to the opposite side of the membrane. <br />
<br />
<br />
<br />
Click '>here</scene> for a view where the different components are coloured differently? See how many you can identify<br />
<br />
<br />
----<br />
'''Q3: What is the location and role of the FO region?'''<br />
<br />
----<br />
<br />
<br />
ATP synthase is an example of a molecular motor.<br />
<br />
Use the Structure to answer the questions below. <br />
<br />
----<br />
'''Q4: How many phosphates does ATP have?'''<br />
----<br />
'''Q5: How many phosphates does ADP have'''<br />
----<br />
<br />
----<br />
<br />
<br />
Key Terms<br />
Aspartic acid<br />
ATP<br />
AMP<br />
ATP synthase<br />
<br />
<br />
</StructureSection><br />
<br />
<br />
<br />
{{Clear}}</div>Alice Clark