https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Hakyong+Kwak 2026-09-26T20:06:52Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1923464 2014-05-02T20:37:34Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A phosphorylates specific serine or threonine residues, which activates or deactivates the protein. Depending on the cell type, different proteins are available for phosphorylation. When activated with cAMP, PKA catalyzes the breakdown of glycogen, inhibits the synthesis of glucose, and promotes the increase of heart rate.In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Overall, this enzyme helps regulate glucose levels,glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd &lt;scene name='58/582909/Be-rs/2'&gt;regulatory subunit&lt;/scene&gt; (R) and a 38-kd &lt;scene name='58/582909/Real_cs/1'&gt;catalytic subunit&lt;/scene&gt; (C). The R dimer contains two cAMP bindng domains and the pseudosubstrate sequence, Arg-Arg-Gly-Ala-Ile. The C subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe binds ATP-Mg2+. This &lt;scene name='58/582909/Catalytic_subunit_1/1'&gt;scene&lt;/scene&gt; shows a catalytic subunit with an inhibitor with a psuedosubstrate bound to the active site and an ATP bound to the adjacent active site. When PKA is enzymatically inactive (absence of cAMP), it is a heterotetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The C subunits are enzymatically active in itself and once released, are free to bind and phosphorylate available substrate proteins. <br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the &lt;scene name='58/582909/Psuedosubstrate/1'&gt;pseudosubstrate&lt;/scene&gt; sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the alanine in place of the serine. The pseudosubstrate binds to PKA through specific interactions. The guanidinium group of the first arginine forms an ion pair with the carboxylate groups of the glutamate residue, Glu 127, of the enzyme, forming a salt bridge. In the same way, the second arginine interacts with two other carboxylate groups, forming two more salt bridges. Two leucine residues of the enzyme form a hydrophobic groove in which the nonpolar side chain of isoleucine fits into. The scene is shown here. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> PKA is inactivated by a feedback mechanism. PKA activates phosphodiesterase, which converts cAMP back to ATP. This reduces the amount of cAMP that can activate PKA. <br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> doi:10.2210/rcsb_pdb/mom_2012_8</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1923463 2014-05-02T20:36:30Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A phosphorylates specific serine or threonine residues, which activates or deactivates the protein. Depending on the cell type, different proteins are available for phosphorylation. When activated with cAMP, PKA catalyzes the breakdown of glycogen, inhibits the synthesis of glucose, and promotes the increase of heart rate.In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Overall, this enzyme helps regulate glucose levels,glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd &lt;scene name='58/582909/Be-rs/2'&gt;regulatory subunit&lt;/scene&gt; (R) and a 38-kd &lt;scene name='58/582909/Real_cs/1'&gt;catalytic subunit&lt;/scene&gt; (C). The R dimer contains two cAMP bindng domains and the pseudosubstrate sequence, Arg-Arg-Gly-Ala-Ile. The C subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe binds ATP-Mg2+. This &lt;scene name='58/582909/Catalytic_subunit_1/1'&gt;scene&lt;/scene&gt; shows a catalytic subunit with an inhibitor with a &lt;scene name='58/582909/Psuedosubstrate/1'&gt;pseudosubstrate&lt;/scene&gt; bound to the active site and an ATP bound to the adjacent active site. When PKA is enzymatically inactive (absence of cAMP), it is a heterotetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The C subunits are enzymatically active in itself and once released, are free to bind and phosphorylate available substrate proteins. <br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the alanine in place of the serine. The pseudosubstrate binds to PKA through specific interactions. The guanidinium group of the first arginine forms an ion pair with the carboxylate groups of the glutamate residue, Glu 127, of the enzyme, forming a salt bridge. In the same way, the second arginine interacts with two other carboxylate groups, forming two more salt bridges. Two leucine residues of the enzyme form a hydrophobic groove in which the nonpolar side chain of isoleucine fits into. The scene is shown here. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> PKA is inactivated by a feedback mechanism. PKA activates phosphodiesterase, which converts cAMP back to ATP. This reduces the amount of cAMP that can activate PKA. <br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> doi:10.2210/rcsb_pdb/mom_2012_8</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1922468 2014-05-01T03:19:43Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A phosphorylates specific serine or threonine residues, which activates or deactivates the protein. Depending on the cell type, different proteins are available for phosphorylation. When activated with cAMP, PKA catalyzes the breakdown of glycogen, inhibits the synthesis of glucose, and promotes the increase of heart rate.In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Overall, this enzyme helps regulate glucose levels,glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory &lt;scene name='58/582909/Rs/1'&gt;regulatory subunit&lt;/scene&gt; (R) and a 38-kd &lt;scene name='58/582909/Cs/1'&gt;catalytic subunit&lt;/scene&gt; (C). The R dimer contains two cAMP bindng domains and the pseudosubstrate sequence, Arg-Arg-Gly-Ala-Ile. The C subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe binds ATP-Mg2+. This &lt;scene name='58/582909/Catalytic_subunit_1/1'&gt;scene&lt;/scene&gt; shows a catalytic subunit with an inhibitor with a &lt;scene name='58/582909/Psuedosubstrate/1'&gt;pseudosubstrate&lt;/scene&gt; bound to the active site and an ATP bound to the adjacent active site. When PKA is enzymatically inactive (absence of cAMP), it is a heterotetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The C subunits are enzymatically active in itself and once released, are free to bind and phosphorylate available substrate proteins. <br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the alanine in place of the serine. The pseudosubstrate binds to PKA through specific interactions. The guanidinium group of the first arginine forms an ion pair with the carboxylate groups of the glutamate residue, Glu 127, of the enzyme, forming a salt bridge. In the same way, the second arginine interacts with two other carboxylate groups, forming two more salt bridges. Two leucine residues of the enzyme form a hydrophobic groove in which the nonpolar side chain of isoleucine fits into. The scene is shown here. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> PKA is inactivated by a feedback mechanism. PKA activates phosphodiesterase, which converts cAMP back to ATP. This reduces the amount of cAMP that can activate PKA. <br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> doi:10.2210/rcsb_pdb/mom_2012_8</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1922467 2014-05-01T03:17:12Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A phosphorylates specific serine or threonine residues, which activates or deactivates the protein. Depending on the cell type, different proteins are available for phosphorylation. When activated with cAMP, PKA catalyzes the breakdown of glycogen, inhibits the synthesis of glucose, and promotes the increase of heart rate.In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Overall, this enzyme helps regulate glucose levels,glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory &lt;scene name='58/582909/Rs/1'&gt;regulatory subunit&lt;/scene&gt; (R) and a 38-kd &lt;scene name='58/582909/Cs/1'&gt;catalytic subunit&lt;/scene&gt; (C). The R dimer contains two cAMP bindng domains and the &lt;scene name='58/582909/Psuedosubstrate/1'&gt;pseudosubstrate&lt;/scene&gt; sequence, Arg-Arg-Gly-Ala-Ile. The C subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe binds ATP-Mg2+. This &lt;scene name='58/582909/Catalytic_subunit_1/1'&gt;scene&lt;/scene&gt; shows a catalytic subunit with an inhibitor with a psuedosequence bound to the active site and an ATP bound to the adjacent active site. When PKA is enzymatically inactive (absence of cAMP), it is a heterotetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The C subunits are enzymatically active in itself and once released, are free to bind and phosphorylate available substrate proteins. <br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the alanine in place of the serine. The pseudosubstrate binds to PKA through specific interactions. The guanidinium group of the first arginine forms an ion pair with the carboxylate groups of the glutamate residue, Glu 127, of the enzyme, forming a salt bridge. In the same way, the second arginine interacts with two other carboxylate groups, forming two more salt bridges. Two leucine residues of the enzyme form a hydrophobic groove in which the nonpolar side chain of isoleucine fits into. The scene is shown here. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> PKA is inactivated by a feedback mechanism. PKA activates phosphodiesterase, which converts cAMP back to ATP. This reduces the amount of cAMP that can activate PKA. <br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> doi:10.2210/rcsb_pdb/mom_2012_8</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1922466 2014-05-01T03:08:44Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A phosphorylates specific serine or threonine residues, which activates or deactivates the protein. Depending on the cell type, different proteins are available for phosphorylation. When activated with cAMP, PKA catalyzes the breakdown of glycogen, inhibits the synthesis of glucose, and promotes the increase of heart rate.In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Overall, this enzyme helps regulate glucose levels,glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory &lt;scene name='58/582909/Regulatory_subunits/1'&gt;regulatory subunit&lt;/scene&gt; (R) and a 38-kd &lt;scene name='58/582909/Catalytic_subunits/1'&gt;catalytic subunit&lt;/scene&gt; (C). The R dimer contains two cAMP bindng domains and the psuedosubstrate sequence, Arg-Arg-Gly-Ala-Ile. The C subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe binds ATP-Mg2+. This &lt;scene name='58/582909/Catalytic_subunit_1/1'&gt;scene&lt;/scene&gt; shows a catalytic subunit with an inhibitor with a &lt;scene name='58/582909/Psuedosubstrate/1'&gt;pseudosubstrate&lt;/scene&gt; bound to the active site and an ATP bound to the adjacent active site. When PKA is enzymatically inactive (absence of cAMP), it is a heterotetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The C subunits are enzymatically active in itself and once released, are free to bind and phosphorylate available substrate proteins. <br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the alanine in place of the serine. The pseudosubstrate binds to PKA through specific interactions. The guanidinium group of the first arginine forms an ion pair with the carboxylate groups of the glutamate residue, Glu 127, of the enzyme, forming a salt bridge. In the same way, the second arginine interacts with two other carboxylate groups, forming two more salt bridges. Two leucine residues of the enzyme form a hydrophobic groove in which the nonpolar side chain of isoleucine fits into. The scene is shown here. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> PKA is inactivated by a feedback mechanism. PKA activates phosphodiesterase, which converts cAMP back to ATP. This reduces the amount of cAMP that can activate PKA. <br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> doi:10.2210/rcsb_pdb/mom_2012_8</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1922465 2014-05-01T03:04:12Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A phosphorylates specific serine or threonine residues, which activates or deactivates the protein. Depending on the cell type, different proteins are available for phosphorylation. When activated with cAMP, PKA catalyzes the breakdown of glycogen, inhibits the synthesis of glucose, and promotes the increase of heart rate.In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Overall, this enzyme helps regulate glucose levels,glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory &lt;scene name='58/582909/Regulatory_subunits/1'&gt;regulatory subunit&lt;/scene&gt; (R) and a 38-kd &lt;scene name='58/582909/Catalytic_subunits/1'&gt;catalytic subunit&lt;/scene&gt; (C). The R dimer contains two cAMP bindng domains and the &lt;scene name='58/582909/Psuedosubstrate/1'&gt;pseudosubstrate&lt;/scene&gt; sequence, Arg-Arg-Gly-Ala-Ile. The C subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe binds ATP-Mg2+. This &lt;scene name='58/582909/Catalytic_subunit_1/1'&gt;scene&lt;/scene&gt; shows a catalytic subunit with an inhibitor with a psuedosequence bound to the active site and an ATP bound to the adjacent active site. When PKA is enzymatically inactive (absence of cAMP), it is a heterotetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The C subunits are enzymatically active in itself and once released, are free to bind and phosphorylate available substrate proteins. <br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the alanine in place of the serine. The pseudosubstrate binds to PKA through specific interactions. The guanidinium group of the first arginine forms an ion pair with the carboxylate groups of the glutamate residue, Glu 127, of the enzyme, forming a salt bridge. In the same way, the second arginine interacts with two other carboxylate groups, forming two more salt bridges. Two leucine residues of the enzyme form a hydrophobic groove in which the nonpolar side chain of isoleucine fits into. The scene is shown here. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> PKA is inactivated by a feedback mechanism. PKA activates phosphodiesterase, which converts cAMP back to ATP. This reduces the amount of cAMP that can activate PKA. <br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> doi:10.2210/rcsb_pdb/mom_2012_8</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1922433 2014-04-30T17:19:50Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A phosphorylates specific serine or threonine residues, which activates or deactivates the protein. Depending on the cell type, different proteins are available for phosphorylation. When activated with cAMP, PKA catalyzes the breakdown of glycogen, inhibits the synthesis of glucose, and promotes the increase of heart rate.In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Overall, this enzyme helps regulate glucose levels,glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory &lt;scene name='58/582909/Regulatory_subunits/1'&gt;regulatory subunit&lt;/scene&gt; (R) and a 38-kd &lt;scene name='58/582909/Catalytic_subunits/1'&gt;catalytic subunit&lt;/scene&gt; (C). The R dimer contains two cAMP bindng domains and the pseudosbustrate sequence, Arg-Arg-Gly-Ala-Ile. The C subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe binds ATP-Mg2+. This &lt;scene name='58/582909/Catalytic_subunit_1/1'&gt;scene&lt;/scene&gt; shows a catalytic subunit with an inhibitor with a psuedosequence bound to the active site and an ATP bound to the adjacent active site. When PKA is enzymatically inactive (absence of cAMP), it is a heterotetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The C subunits are enzymatically active in itself and once released, are free to bind and phosphorylate available substrate proteins. <br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the alanine in place of the serine. The pseudosubstrate binds to PKA through specific interactions. The guanidinium group of the first arginine forms an ion pair with the carboxylate groups of the glutamate residue, Glu 127, of the enzyme, forming a salt bridge. In the same way, the second arginine interacts with two other carboxylate groups, forming two more salt bridges. Two leucine residues of the enzyme form a hydrophobic groove in which the nonpolar side chain of isoleucine fits into. The scene is shown here. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> PKA is inactivated by a feedback mechanism. PKA activates phosphodiesterase, which converts cAMP back to ATP. This reduces the amount of cAMP that can activate PKA. <br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> doi:10.2210/rcsb_pdb/mom_2012_8</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1922432 2014-04-30T17:17:28Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A phosphorylates specific serine or threonine residues, which activates or deactivates the protein. Depending on the cell type, different proteins are available for phosphorylation. When activated with cAMP, PKA catalyzes the breakdown of glycogen, inhibits the synthesis of glucose, and promotes the increase of heart rate.In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Overall, this enzyme helps regulate glucose levels,glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory &lt;scene name='58/582909/Regulatory_subunits/1'&gt;regulatory subunit&lt;/scene&gt; (R) and a 38-kd &lt;scene name='58/582909/Catalytic_subunits/1'&gt;catalytic subunit&lt;/scene&gt; (C). The R dimer contains two cAMP bindng domains and the pseudosbustrate sequence, Arg-Arg-Gly-Ala-Ile. The C subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe binds ATP-Mg2+. This &lt;scene name='58/582909/Catalytic_subunit_1/1'&gt;scene&lt;/scene&gt; shows a catalytic subunit with an ATP bound to its active site and an inhibitor with a psuedosequence. When PKA is enzymatically inactive (absence of cAMP), it is a heterotetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The C subunits are enzymatically active in itself and once released, are free to bind and phosphorylate available substrate proteins. <br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the alanine in place of the serine. The pseudosubstrate binds to PKA through specific interactions. The guanidinium group of the first arginine forms an ion pair with the carboxylate groups of the glutamate residue, Glu 127, of the enzyme, forming a salt bridge. In the same way, the second arginine interacts with two other carboxylate groups, forming two more salt bridges. Two leucine residues of the enzyme form a hydrophobic groove in which the nonpolar side chain of isoleucine fits into. The scene is shown here. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> PKA is inactivated by a feedback mechanism. PKA activates phosphodiesterase, which converts cAMP back to ATP. This reduces the amount of cAMP that can activate PKA. <br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> doi:10.2210/rcsb_pdb/mom_2012_8</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1922414 2014-04-30T14:11:37Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A phosphorylates specific serine or threonine residues, which activates or deactivates the protein. Depending on the cell type, different proteins are available for phosphorylation. When activated with cAMP, PKA catalyzes the breakdown of glycogen, inhibits the synthesis of glucose, and promotes the increase of heart rate.In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Overall, this enzyme helps regulate glucose levels,glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory &lt;scene name='58/582909/Regulatory_subunits/1'&gt;regulatory subunit&lt;/scene&gt; (R) and a 38-kd &lt;scene name='58/582909/Catalytic_subunits/1'&gt;catalytic subunit&lt;/scene&gt; (C). The R dimer contains two cAMP bindng domains and the pseudosbustrate sequence, Arg-Arg-Gly-Ala-Ile. The C subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe binds ATP-Mg2+. When PKA is enzymatically inactive (absence of cAMP), it is a heterotetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The C subunits are enzymatically active in itself and once released, are free to bind and phosphorylate available substrate proteins. <br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the alanine in place of the serine. The pseudosubstrate binds to PKA through specific interactions. The guanidinium group of the first arginine forms an ion pair with the carboxylate groups of the glutamate residue, Glu 127, of the enzyme, forming a salt bridge. In the same way, the second arginine interacts with two other carboxylate groups, forming two more salt bridges. Two leucine residues of the enzyme form a hydrophobic groove in which the nonpolar side chain of isoleucine fits into. The scene is shown here. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> PKA is inactivated by a feedback mechanism. PKA activates phosphodiesterase, which converts cAMP back to ATP. This reduces the amount of cAMP that can activate PKA. <br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> doi:10.2210/rcsb_pdb/mom_2012_8</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918873 2014-04-29T16:59:36Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. PKA also helps regulate glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory &lt;scene name='58/582909/Regulatory_subunits/1'&gt;regulatory subunit&lt;/scene&gt; (R) and a 38-kd &lt;scene name='58/582909/Catalytic_subunits/1'&gt;catalytic subunit&lt;/scene&gt; (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the alanine in place of the serine. The pseudosubstrate binds to PKA through specific interactions. The guanidinium group of the first arginine forms an ion pair with the carboxylate groups of the glutamate residue, Glu 127, of the enzyme, forming a salt bridge. In the same way, the second arginine interacts with two other carboxylate groups, forming two more salt bridges. Two leucine residues of the enzyme form a hydrophobic groove in which the nonpolar side chain of isoleucine fits into. The scene is shown here. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> PKA is inactivated by a feedback mechanism. PKA activates phosphodiesterase, which converts cAMP back to ATP. This reduces the amount of cAMP that can activate PKA. <br /> <br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> doi:10.2210/rcsb_pdb/mom_2012_8</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918872 2014-04-29T16:53:57Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. PKA also helps regulate glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory &lt;scene name='58/582909/Regulatory_subunits/1'&gt;regulatory subunit&lt;/scene&gt; (R) and a 38-kd &lt;scene name='58/582909/Catalytic_subunits/1'&gt;catalytic subunit&lt;/scene&gt; (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the alanine in place of the serine. The pseudosubstrate binds to PKA through specific interactions. The guanidinium group of the first arginine forms an ion pair with the carboxylate groups of the glutamate residue, Glu 127, of the enzyme, forming a salt bridge. In the same way, the second arginine interacts with two other carboxylate groups, forming two more salt bridges. Two leucine residues of the enzyme form a hydrophobic groove in which the nonpolar side chain of isoleucine fits into. The scene is shown here. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> [doi:10.2210/rcsb_pdb/mom_2012_8]</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918865 2014-04-29T15:37:25Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='3tnp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. PKA also helps regulate glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory &lt;scene name='58/582909/Regulatory_subunits/1'&gt;regulatory subunit&lt;/scene&gt;)(R) and a 38-kd &lt;scene name='58/582909/Catalytic_subunits/1'&gt;catalytic subunit&lt;/scene&gt; (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the Alanine in place of the serine. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> [doi:10.2210/rcsb_pdb/mom_2012_8]</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918864 2014-04-29T15:35:10Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. PKA also helps regulate glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory &lt;scene name='58/582909/Regulatory_subunits/1'&gt;TextToBeDisplayed&lt;/scene&gt;) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the Alanine in place of the serine. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> [doi:10.2210/rcsb_pdb/mom_2012_8]</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918863 2014-04-29T14:32:19Z

<p>Hakyong Kwak: </p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. PKA also helps regulate glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the Alanine in place of the serine. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)<br /> [doi:10.2210/rcsb_pdb/mom_2012_8]</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918395 2014-04-27T02:40:12Z

<p>Hakyong Kwak: /* &#039;Protein kinase A (PKA)&#039; */</p> <hr /> <div>==Protein kinase A (PKA)==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. PKA also helps regulate glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the Alanine in place of the serine. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918393 2014-04-27T02:39:43Z

<p>Hakyong Kwak: /* Your Heading Here (maybe something like &#039;Protein kinase A (PKA)&#039;) */</p> <hr /> <div>=='Protein kinase A (PKA)'==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. PKA also helps regulate glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the Alanine in place of the serine. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918392 2014-04-27T02:39:21Z

<p>Hakyong Kwak: /* Your Heading Here (maybe something like &#039;Structure&#039;) */</p> <hr /> <div>==Your Heading Here (maybe something like 'Protein kinase A (PKA)')==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase.<br /> <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. PKA also helps regulate glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the Alanine in place of the serine. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918390 2014-04-27T02:36:57Z

<p>Hakyong Kwak: </p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase. <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. PKA also helps regulate glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> <br /> == Mechanism ==<br /> PKA consists of a regulatory dimer, which each regulatory subunit attached to a catalytic subunit. When cAMP levels are low, the enzyme is intact, forming the R2C2 complex. However, when cAMP levels are high, two cAMP molecules bind to the regulatory sites of the complex, which leads to the dissociation of the R2C2 complex into an R2 subunit and two C subunits. When cAMP binds to the R chains, the binding allosterically removes the pseudostubstrate sequences, Arg-Arg-Gly-Ala-Ile, out of the catalytic sites. This psuedosubstrate sequence of R occupies the catalytic site of C and prevents it from interacting with protein substrates. The only difference between the pseudosubstrate sequence and the sequence for phophorylations is the Alanine in place of the serine. Once released, the two enzymatically active C subunites are free to phosphorylate proteins. <br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918367 2014-04-26T23:18:11Z

<p>Hakyong Kwak: </p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase. <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. PKA also helps regulate glycogen levels, sugar levels, and lipid metabolism. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> == Mechanism ==<br /> <br /> == Regulation ==<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918366 2014-04-26T23:15:54Z

<p>Hakyong Kwak: </p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase. <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> == Mechanism ==<br /> <br /> == Regulation ==<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1918365 2014-04-26T23:15:26Z

<p>Hakyong Kwak: </p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Protein kinase A (PKA)' scene=''&gt;<br /> is is a default text for your page '''Protein kinase A (PKA)''' is a group of enzymes whose activity is dependent on the concentration of cAMP, and is also known as cAMP-dependent protein kinase. <br /> == Function ==<br /> Protein kinase A is Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscles become ready for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> == Mechanism ==<br /> <br /> == Regulation ==<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1915297 2014-04-22T03:20:34Z

<p>Hakyong Kwak: </p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''Protein Kinase A'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscle becomes primed for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. (? makes sure this is right)<br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> == Mechanism ==<br /> <br /> == Regulation ==<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> [1]Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644<br /> [2]C. Kim, N.-H. Xuong, and S.S. Taylor, &quot;Crystal structure of a complex between catalytic and regulatory (Rlα) subunits of PKA,&quot;Science 307, 690 (2005)</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1915296 2014-04-22T03:19:26Z

<p>Hakyong Kwak: </p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''Protein Kinase A'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscle becomes primed for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. (? makes sure this is right)<br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> == Mechanism ==<br /> <br /> == Regulation ==<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1915295 2014-04-22T03:16:12Z

<p>Hakyong Kwak: </p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''Protein Kinase A'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscle becomes primed for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. <br /> <br /> == Structure ==<br /> PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.<br /> == Mechanism ==<br /> <br /> == Regulation ==<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1915294 2014-04-22T02:42:41Z

<p>Hakyong Kwak: </p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''Protein Kinase A'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Protein Kinase A (PKA) helps animals cope with stressful situations. In the &quot;flight or fight&quot; response, muscle becomes primed for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. <br /> <br /> == Mechanism ==<br /> <br /> == Regulation ==<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1915293 2014-04-22T02:33:42Z

<p>Hakyong Kwak: </p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''Protein Kinase A'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; 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 &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644</div>

Hakyong Kwak https://proteopedia.org/index.php?title=Protein_Kinase_A&diff=1915289 2014-04-22T02:18:34Z

<p>Hakyong Kwak: New page: ==Your Heading Here (maybe something like &#039;Structure&#039;)== &lt;StructureSection load=&#039;1atp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&gt; This is a default text for you...</p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1atp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''Protein Kinase A'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; 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 &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Hakyong Kwak https://proteopedia.org/index.php?title=NADH:ubiquinone_oxidoreductase&diff=1915266 2014-04-21T17:55:21Z

<p>Hakyong Kwak: </p> <hr /> <div>==Structure==<br /> &lt;StructureSection load='3m9s' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''NADH:ubiquinone oxidoreductase'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Complex I is the first enzyme of the electron transport chain. This enzyme is one of the three large chains of protein complexes that electrons are transferred through. For every molecule of NADH that is oxidized, this complex moves four protons across the inner membrane and into the cytoplasm. This helps build the electrochemical potential used to produce ATP. The reaction of this complex is NADH + Q + 5H+(matrix) → NAD+ + QH2 + 4H+(cytoplasm)<br /> <br /> ==Mechanism==<br /> NADH initially binds to Complex I and transfers its two electrons to the flavin mononucleotide (FMN) prosthetic group, reducing its form to FMNH2. These electrons flow through a series of Fe-S centers and then to coenzyme Q. This flow leads to the pumping of four hydrogen ions out of the matrix of the mitochondria. Q, upon accepting the two electrons, takes up two protons from the matrix and is reduced to QH2. All redox reactions take place in the extramembraneous part (hydrophillic) of NADH-Q oxidoreductase. <br /> <br /> == Structure ==<br /> NADH-Q oxidoreductase consists of approximately 46 polypeptide chains (&gt;900kd). The genes encoding this proton pump resides in both the mitochondria and the nucleus. This enzyme is L-shaped, with a horizontal arm lying the membrane and a vertical arm that projects into the matrix. <br /> <br /> == Disease ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644</div>

Hakyong Kwak https://proteopedia.org/index.php?title=NADH:ubiquinone_oxidoreductase&diff=1915243 2014-04-21T04:23:15Z

<p>Hakyong Kwak: </p> <hr /> <div>==Structure==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''NADH:ubiquinone oxidoreductase'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Complex I is the first enzyme of the electron transport chain. This enzyme is one of the three large chains of protein complexes that electrons are transferred through. For every molecule of NADH that is oxidized, this complex moves four protons across the inner membrane and into the cytoplasm. This helps build the electrochemical potential used to produce ATP. The reaction of this complex is NADH + Q + 5H+(matrix) → NAD+ + QH2 + 4H+(cytoplasm)<br /> <br /> ==Mechanism==<br /> NADH initially binds to Complex I and transfers its two electrons to the flavin mononucleotide (FMN) prosthetic group, reducing its form to FMNH2. These electrons flow through a series of Fe-S centers and then to coenzyme Q. This flow leads to the pumping of four hydrogen ions out of the matrix of the mitochondria. Q, upon accepting the two electrons, takes up two protons from the matrix and is reduced to QH2. All redox reactions take place in the extramembraneous part (hydrophillic) of NADH-Q oxidoreductase. <br /> <br /> == Structure ==<br /> NADH-Q oxidoreductase consists of approximately 46 polypeptide chains (&gt;900kd). The genes encoding this proton pump resides in both the mitochondria and the nucleus. This enzyme is L-shaped, with a horizontal arm lying the membrane and a vertical arm that projects into the matrix. <br /> <br /> == Disease ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644</div>

Hakyong Kwak https://proteopedia.org/index.php?title=NADH:ubiquinone_oxidoreductase&diff=1915242 2014-04-21T04:20:44Z

<p>Hakyong Kwak: </p> <hr /> <div>==Structure==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''NADH:ubiquinone oxidoreductase'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Complex I is the first enzyme of the electron transport chain. This enzyme is one of the three large chains of protein complexes that electrons are transferred through. For every molecule of NADH that is oxidized, this complex moves four protons across the inner membrane and into the cytoplasm. This helps build the electrochemical potential used to produce ATP. The reaction of this complex is NADH + Q + 5H+(matrix) → NAD+ + QH2 + 4H+(cytoplasm)<br /> <br /> ==Mechanism==<br /> NADH initially binds to Complex I and transfers its two electrons to the flavin mononucleotide (FMN) prosthetic group, reducing its form to FMNH2. These electrons flow through a series of Fe-S centers and then to coenzyme Q. This flow leads to the pumping of four protons out of the matrix of the mitochondria. All redox reactions take place in the extramembraneous part (hydrophillic) of NADH-Q oxidoreductase. <br /> <br /> == Structure ==<br /> NADH-Q oxidoreductase consists of approximately 46 polypeptide chains (&gt;900kd). The genes encoding this proton pump resides in both the mitochondria and the nucleus. This enzyme is L-shaped, with a horizontal arm lying the membrane and a vertical arm that projects into the matrix. <br /> <br /> == Disease ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644</div>

Hakyong Kwak https://proteopedia.org/index.php?title=NADH:ubiquinone_oxidoreductase&diff=1915241 2014-04-21T04:14:12Z

<p>Hakyong Kwak: </p> <hr /> <div>==Structure==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''NADH:ubiquinone oxidoreductase'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Complex I is the first enzyme of the electron transport chain. This enzyme is one of the three large chains of protein complexes that electrons are transferred through. For every molecule of NADH that is oxidized, this complex moves four protons across the inner membrane and into the cytoplasm. This helps build the electrochemical potential used to produce ATP. The reaction of this complex is NADH + Q + 5H+(matrix) → NAD+ + QH2 + 4H+(cytoplasm)<br /> <br /> == Structure ==<br /> NADH-Q oxidoreductase consists of approximately 46 polypeptide chains (&gt;900kd). The genes encoding this proton pump resides in both the mitochondria and the nucleus. This enzyme is L-shaped, with a horizontal arm lying the membrane and a vertical arm that projects into the matrix. <br /> <br /> == Disease ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644</div>

Hakyong Kwak https://proteopedia.org/index.php?title=NADH:ubiquinone_oxidoreductase&diff=1915240 2014-04-21T04:10:35Z

<p>Hakyong Kwak: </p> <hr /> <div>==Structure==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''NADH:ubiquinone oxidoreductase'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Complex I is the first enzyme of the electron transport chain. This enzyme is one of the three large chains of protein complexes that electrons are transferred through. For every molecule of oxidized NADH, this complex translocates four protons across the inner membrane. This helps build the electrochemical potential used to produce ATP. The reaction of this complex is NADH + Q + 5H+matrix → NAD+ + QH2 + 4H+cytoplasm<br /> <br /> == Structure ==<br /> NADH-Q oxidoreductase consists of approximately 46 polypeptide chains (&gt;900kd). The genes encoding this proton pump resides in both the mitochondria and the nucleus. This enzyme is L-shaped, with a horizontal arm lying the membrane and a vertical arm that projects into the matrix. <br /> <br /> == Disease ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644</div>

Hakyong Kwak https://proteopedia.org/index.php?title=NADH:ubiquinone_oxidoreductase&diff=1915239 2014-04-21T04:10:09Z

<p>Hakyong Kwak: </p> <hr /> <div>==Structure==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''NADH:ubiquinone oxidoreductase'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Complex I is the first enzyme of the electron transport chain. This enzyme is one of the three large chains of protein complexes that electrons are transferred through. For every molecule of oxidized NADH, this complex translocates four protons across the inner membrane. This helps build the electrochemical potential used to produce ATP. The reaction of this complex is NADH + Q + 5H+matrix → NAD+ + QH2 + 4H+cytoplasm<br /> <br /> == Structure ==<br /> NADH-Q oxidoreductase consists of approximately 46 polypeptide chains (&gt;900kd). The genes encoding this proton pump resides in both the mitochondria and the nucleus. This enzyme is L-shaped, with a horizontal arm lying the membrane and a vertical arm that projects into the matrix. <br /> <br /> == Disease ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644/&gt;</div>

Hakyong Kwak https://proteopedia.org/index.php?title=NADH:ubiquinone_oxidoreductase&diff=1915238 2014-04-21T04:05:07Z

<p>Hakyong Kwak: </p> <hr /> <div>==Structure==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''NADH:ubiquinone oxidoreductase'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Complex I is the first enzyme of the electron transport chain. This enzyme is one of the three large chains of protein complexes that electrons are transferred through. For every molecule of oxidized NADH, this complex translocates four protons across the inner membrane. This helps build the electrochemical potential used to produce ATP. The reaction of this complex is NADH + Q + 5H+matrix → NAD+ + QH2 + 4H+cytoplasm<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Hakyong Kwak https://proteopedia.org/index.php?title=NADH:ubiquinone_oxidoreductase&diff=1915237 2014-04-21T04:01:35Z

<p>Hakyong Kwak: /* Your Heading Here (maybe something like &#039;Structure&#039;) */</p> <hr /> <div>==Structure==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''NADH:ubiquinone oxidoreductase'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Complex I is the first enzyme of the electron transport chain. This enzyme is one of the three large chains of protein complexes that electrons are transferred through. For every molecule of oxidized NADH, this complex translocates four protons across the inner membrane. This helps build the electrochemical potential used to produce ATP. The reaction of this complex is<br /> NADH + H+ + CoQ + 4H+in → NAD+ + CoQH2 + 4H+out<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Hakyong Kwak https://proteopedia.org/index.php?title=NADH:ubiquinone_oxidoreductase&diff=1915236 2014-04-21T03:53:35Z

<p>Hakyong Kwak: New page: ==Your Heading Here (maybe something like &#039;Structure&#039;)== &lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&gt; This is a default text for you...</p> <hr /> <div>==Your Heading Here (maybe something like 'Structure')==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''NADH:ubiquinone oxidoreductase'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> Complex I is the first enzyme of the electron transport chain. This enzyme is one of the three large chains of protein complexes that electrons are transferred through. For every molecule of oxidized NADH, this complex translocates four protons across the inner membrane. This helps build the electrochemical potential used to produce ATP. The reaction of this complex is<br /> NADH + H+ + CoQ + 4H+in → NAD+ + CoQH2 + 4H+out<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; 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 /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Hakyong Kwak