https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Kevin+JohnsonProteopedia - User contributions [en]2026-09-21T20:36:57ZUser contributionsMediaWiki 1.43.8https://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3759039Sandbox Reserved 18022023-04-27T15:34:06Z<p>Kevin Johnson: </p>
<hr />
<div><scene name='95/954099/Hydrogen_bonds/4'>Text To Be Displayed</scene>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
== Biological relevance and broader implications ==<br />
Not much is known about the futalosine pathway and the way it works. MqnA is the first enzyme of the futalosine pathway catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), a reaction not observed for any other enzyme. Chorismate is the product of the shikimate pathway and the precursor of many aromatic compounds including the amino acids in addition to the electron carriers ubiquinone and menaquinone. As enzymes of the shikimate pathway, as well as enzymes that convert chorismate, are only present in bacteria, fungi, and plants, they are promising targets for antimicrobials and herbicides. <br />
== Important amino acids==<br />
The catalytic amino acids in my enzyme are ALA18, SER87, and TYR243. These three amino acids would be considered the <scene name='95/954099/New_triad/2'>catalytic triad</scene>.<br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/4'>THR60, SER87, CYS88, SER110, ARG111, THR112, SER113, GLY152.</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR60, SER87, CYS88, SER110, ARG111, THR112, SER113, GLY152, PHE187, THR243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO42, VAL79, VAL85, ILE151, PHE187<br />
== Structural highlights ==<br />
<br />
The Secondary structures has 20 beta sheets, 28 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by <scene name='95/954099/Structural_highlights/1'>two linkers</scene>. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/8'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3759001Sandbox Reserved 18022023-04-26T21:48:49Z<p>Kevin Johnson: </p>
<hr />
<div><scene name='95/954099/Hydrogen_bonds/4'>Text To Be Displayed</scene>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
== Biological relevance and broader implications ==<br />
Not much is known about the futalosine pathway and the way it works. MqnA is the first enzyme of the futalosine pathway catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), a reaction not observed for any other enzyme. Chorismate is the product of the shikimate pathway and the precursor of many aromatic compounds including the amino acids in addition to the electron carriers ubiquinone and menaquinone. As enzymes of the shikimate pathway, as well as enzymes that convert chorismate, are only present in bacteria, fungi, and plants, they are promising targets for antimicrobials and herbicides. <br />
== Important amino acids==<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be considered the <scene name='95/954099/New_triad/2'>catalytic triad</scene>.<br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/4'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151.</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
== Structural highlights ==<br />
<br />
The Secondary structures has 20 beta sheets, 28 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by <scene name='95/954099/Structural_highlights/1'>two linkers</scene>. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/8'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758999Sandbox Reserved 18022023-04-26T21:22:23Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
== Biological relevance and broader implications ==<br />
Not much is known about the futalosine pathway and the way it works. MqnA is the first enzyme of the futalosine pathway catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), a reaction not observed for any other enzyme. Chorismate is the product of the shikimate pathway and the precursor of many aromatic compounds including the amino acids in addition to the electron carriers ubiquinone and menaquinone. As enzymes of the shikimate pathway, as well as enzymes that convert chorismate, are only present in bacteria, fungi, and plants, they are promising targets for antimicrobials and herbicides. <br />
== Important amino acids==<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be considered the <scene name='95/954099/New_triad/2'>catalytic triad</scene>.<br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
== Structural highlights ==<br />
<br />
The Secondary structures has 20 beta sheets, 28 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by <scene name='95/954099/Structural_highlights/1'>two linkers</scene>. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/8'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758998Sandbox Reserved 18022023-04-26T20:49:30Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
== Biological relevance and broader implications ==<br />
Not much is known about the futalosine pathway and the way it works. MqnA is the first enzyme of the futalosine pathway catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), a reaction not observed for any other enzyme. Chorismate is the product of the shikimate pathway and the precursor of many aromatic compounds including the amino acids in addition to the electron carriers ubiquinone and menaquinone. As enzymes of the shikimate pathway, as well as enzymes that convert chorismate, are only present in bacteria, fungi, and plants, they are promising targets for antimicrobials and herbicides. <br />
== Important amino acids==<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
== Structural highlights ==<br />
<br />
The Secondary structures has 20 beta sheets, 28 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by <scene name='95/954099/Structural_highlights/1'>two linkers</scene>. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/8'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758997Sandbox Reserved 18022023-04-26T20:45:45Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
<br />
Not much is known about the futalosine pathway and the way it works. MqnA is the first enzyme of the futalosine pathway catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), a reaction not observed for any other enzyme. Chorismate is the product of the shikimate pathway and the precursor of many aromatic compounds including the amino acids in addition to the electron carriers ubiquinone and menaquinone. As enzymes of the shikimate pathway, as well as enzymes that convert chorismate, are only present in bacteria, fungi, and plants, they are promising targets for antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has 20 beta sheets, 28 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by <scene name='95/954099/Structural_highlights/1'>two linkers</scene>. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/8'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758996Sandbox Reserved 18022023-04-26T20:28:27Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
<br />
Not much is known about the futalosine pathway and the way it works. MqnA is the first enzyme of the futalosine pathway catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), a reaction not observed for any other enzyme. Chorismate is the product of the shikimate pathway and the precursor of many aromatic compounds including the amino acids in addition to the electron carriers ubiquinone and menaquinone. As enzymes of the shikimate pathway, as well as enzymes that convert chorismate, are only present in bacteria, fungi, and plants, they are promising targets for antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 20 beta sheets, 28 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by <scene name='95/954099/View_2/2'>two linkers</scene>. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/8'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758995Sandbox Reserved 18022023-04-26T20:13:22Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
<br />
Not much is known about the futalosine pathway and the way it works. MqnA is the first enzyme of the futalosine pathway catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), a reaction not observed for any other enzyme. Chorismate is the product of the shikimate pathway and the precursor of many aromatic compounds including the amino acids in addition to the electron carriers ubiquinone and menaquinone. As enzymes of the shikimate pathway, as well as enzymes that convert chorismate, are only present in bacteria, fungi, and plants, they are promising targets for antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/8'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758994Sandbox Reserved 18022023-04-26T20:01:48Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for.<br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/8'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758993Sandbox Reserved 18022023-04-26T19:17:28Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/8'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758992Sandbox Reserved 18022023-04-26T19:12:02Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/8'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/4'>A different view of the deep cleft.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758991Sandbox Reserved 18022023-04-26T19:02:48Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree.<scene name='95/954099/Cleft/7'> Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/4'>A different view of the deep cleft.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758989Sandbox Reserved 18022023-04-26T18:53:05Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/3'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/4'>A different view of the deep cleft.</scene> <scene name='95/954099/Cleft/5'>Opening and Closing of the VFT fold.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758988Sandbox Reserved 18022023-04-26T18:28:05Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/3'>Deep cleft in center of enzyme.</scene> <scene name='95/954099/Cleft/4'>A different view of the deep cleft.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758987Sandbox Reserved 18022023-04-26T18:13:41Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/3'>Deep cleft in center of enzyme.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3758785Sandbox Reserved 18022023-04-26T18:02:45Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. <scene name='95/954099/Cleft/1'>Deep cleft in center of enzyme.</scene><br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755983Sandbox Reserved 18022023-04-25T18:00:32Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ALA17, SER86, and PHE243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. /Users/kevinjohnson/Desktop/VFT Pic.png<br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755982Sandbox Reserved 18022023-04-25T17:58:55Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ASN17, SER86, and TYR243. These three amino acids would be <scene name='95/954099/Triad/1'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, TYR242<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. /Users/kevinjohnson/Desktop/VFT Pic.png<br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755940Sandbox Reserved 18022023-04-24T20:26:28Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ASN17, SER86, and TYR243. These three amino acids would be the <scene name='95/954099/Catalytic_triad/6'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, TYR242<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. /Users/kevinjohnson/Desktop/VFT Pic.png<br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755939Sandbox Reserved 18022023-04-24T20:24:51Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ASN17, SER86, and TYR243. These three amino acids would be the <scene name='95/954099/Catalytic_triad/6'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, TYR242<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. [[Image:Example.jpg]]<br />
<br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755938Sandbox Reserved 18022023-04-24T20:23:53Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ASN17, SER86, and TYR243. These three amino acids would be the <scene name='95/954099/Catalytic_triad/6'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, TYR242<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15 degree without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7 degree. VFT Pic<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755937Sandbox Reserved 18022023-04-24T20:14:29Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ASN17, SER86, and TYR243. These three amino acids would be the <scene name='95/954099/Catalytic_triad/6'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene><br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, TYR242<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15o without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7o.<br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755919Sandbox Reserved 18022023-04-24T16:45:16Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ASN17, SER86, and TYR242. These three amino acids would be the <scene name='95/954099/Catalytic_triad/6'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: <scene name='95/954099/Hydrogen_bonds/3'>THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151</scene><br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, PHE186, LEU246<br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, TYR242<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15o without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7o.<br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755910Sandbox Reserved 18022023-04-24T13:56:23Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ASN17, SER86, and TYR242. These three amino acids would be the <scene name='95/954099/Catalytic_triad/6'>catalytic triad.</scene><br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151<br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, PHE186, LEU246<br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, TYR242<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15o without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7o.<br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755893Sandbox Reserved 18022023-04-24T11:32:59Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for <scene name='95/954099/View_2/1'>potential antimicrobials and herbicides.</scene><br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ARG17, SER86, and TYR242. These three amino acids would be the catalytic triad.<br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151<br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, PHE186, LEU246<br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, TYR242<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15o without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7o.<br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755891Sandbox Reserved 18022023-04-24T11:25:17Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are <scene name='95/954099/Protein_view_2/5'>promising targets for potential antimicrobials and herbicides.</scene> <br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ARG17, SER86, and TYR242. These three amino acids would be the catalytic triad.<br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151<br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, PHE186, LEU246<br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, TYR242<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15o without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7o.<br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755890Sandbox Reserved 18022023-04-24T11:24:38Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are <scene name='95/954099/Protein_view_2/5'>promising targets for potential antimicrobials and herbicides.</scene> <br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ARG17, SER86, and TYR242. These three amino acids would be the catalytic triad.<br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151<br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, PHE186, LEU246<br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, TYR242<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
== Other Important Features ==<br />
<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15o without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7o.<br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3755889Sandbox Reserved 18022023-04-24T11:10:30Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
My protein is found in the Streptomyces coelicolor, but being expressed system in Escherichia coli. The specific function of Chorismate dehydratase is to catalyze the dehydration of chorismate to produce 3-enolpyruvyl-benzoate (3-EPB). Chorismate dehydratase has two ligands, both are (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid (ISJ). The two ISJ molecules are on different of lobes of Chorismate dehydratase (Lobe A and Lobe B). <br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are <scene name='95/954099/Protein_view_2/5'>promising targets for potential antimicrobials and herbicides.</scene> <br />
<br />
== Important amino acids==<br />
<br />
The catalytic amino acids in my enzyme are ARG17, SER86, and TYR242. These three amino acids would be the catalytic triad.<br />
<br />
ISJ (A) has the following Hydrogen bonds with ScMqnA: THR59, SER86, CYS87, SER109, ARG110, THR111, SER112, GLY151<br />
ISJ (A) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, PHE186, LEU246<br />
<br />
ISJ (B) has the following Hydrogen bonds with ScMqnA: THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, TYR242<br />
ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO41, VAL78, VAL84, ILE150, PHE186<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
Other important features:<br />
<br />
Chorismate dehydratas uses a Venus flytrap (VFT) fold found typically in ligand binding proteins, the degree of opening/closing in MqnA appears to be different compared to nonenzymatic structural neighbors. A characteristic feature of VFT proteins is the ligand-mediated switching between an open ligand-free and a closed ligand-bound structure. The typical rotation would be about 15o without significant structural changes within the separate lobe domains. In contrast, the rotation angle between the two lobe domains accounts only for 7o.<br />
<br />
Chorismate dehydratase is also a homo dimer which means that both of its lobes have the same amount of amino acids and are structurally identical. The dimer is formed mostly by interactions of the N-terminal amino acids with helix α11 and the subsequent loop of the second molecule, as well as of amino acids 19 to 38 (containing β2 and α1) with the equivalent region of the second molecule. The dimer interface is distant from the active site and from the moving regions in VFT proteins, it’s not expected to influence catalysis. <br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748737Sandbox Reserved 18022023-04-09T18:13:28Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are <scene name='95/954099/Protein_view_2/5'>promising targets for potential antimicrobials and herbicides.</scene> <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the catalytic triad are N17, S86, and Y242.<br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
The Secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball, with an alpha clamp and two lobes connected by two linkers. The beta sheets contain all three of the catalytic amino acids and most of the important binding amino acids.<br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748679Sandbox Reserved 18022023-04-08T19:47:31Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are <scene name='95/954099/Protein_view_2/5'>promising targets for potential antimicrobials and herbicides.</scene> <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the catalytic triad are N17, S86, and Y242.<br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
Chorismate dehydratase’s secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball that includes an alpha clamp and two lobes connected by two linkers.<br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748678Sandbox Reserved 18022023-04-08T19:02:39Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the catalytic triad ar<scene name='95/954099/Catalytic_triad/1'>e N17,S86, and Y242</scene>.<br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
Chorismate dehydratase’s secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball that includes an alpha clamp and two lobes connected by two linkers.<br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748438Sandbox Reserved 18022023-04-07T15:08:48Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
Chorismate dehydratase’s secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball that includes an alpha clamp and two lobes connected by two linkers.<br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748437Sandbox Reserved 18022023-04-07T15:06:37Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
Chorismate dehydratase’s secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball that includes an alpha clamp and two lobes connected by two linkers.<br />
<br />
</StructureSection><br />
== References ==<br />
<ref>PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748435Sandbox Reserved 18022023-04-07T15:03:47Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
Chorismate dehydratase’s secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball that includes an alpha clamp and two lobes connected by two linkers.<br />
<br />
</StructureSection><br />
== References ==<br />
<ref>PMID:36265588</ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748434Sandbox Reserved 18022023-04-07T15:03:09Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
Chorismate dehydratase’s secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball that includes an alpha clamp and two lobes connected by two linkers.<br />
<br />
</StructureSection><br />
== References ==<br />
<ref> PMID:36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748431Sandbox Reserved 18022023-04-07T14:59:59Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
Chorismate dehydratase’s secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball that includes an alpha clamp and two lobes connected by two linkers.<br />
<br />
</StructureSection><br />
== References ==<br />
<ref>PMID: 36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748430Sandbox Reserved 18022023-04-07T14:59:13Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
Chorismate dehydratase’s secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball that includes an alpha clamp and two lobes connected by two linkers.<br />
<br />
</StructureSection><br />
== References ==<br />
<ref>PMID:36265588 </ref><br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748427Sandbox Reserved 18022023-04-07T14:54:16Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
Chorismate dehydratase’s secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball that includes an alpha clamp and two lobes connected by two linkers.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748407Sandbox Reserved 18022023-04-07T14:25:11Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
Chorismate dehydratase’s secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball that includes an alpha clamp and two lobes connected by two linkers.<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748394Sandbox Reserved 18022023-04-07T13:06:47Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway.<br />
<br />
== Biological relevance and broader implications ==<br />
Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. <br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748391Sandbox Reserved 18022023-04-07T12:58:50Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB).<br />
<br />
My protein could have some<scene name='95/954099/Protein_view_2/1'> important future antibiotic use.</scene> <br />
== Biological relevance and broader implications ==<br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748388Sandbox Reserved 18022023-04-07T12:37:46Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
<br />
My protein could have some<scene name='95/954099/Protein_view_2/1'> important future antibiotic use.</scene> <br />
== Biological relevance and broader implications ==<br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748387Sandbox Reserved 18022023-04-07T12:31:11Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
== Chorismate dehydratase (MqnA) ==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
<br />
My protein could have some<scene name='95/954099/Protein_view_2/1'> important future antibiotic use.</scene> <br />
== Biological relevance and broader implications ==<br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748386Sandbox Reserved 18022023-04-07T11:54:58Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
<br />
My protein could have some<scene name='95/954099/Protein_view_2/1'> important future antibiotic use.</scene> <br />
== Biological relevance and broader implications ==<br />
<br />
== Important amino acids==<br />
<br />
The three amnio acids involved in the <scene name='95/954099/Catalytic_traid/1'>catalytic triad.</scene><br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748385Sandbox Reserved 18022023-04-07T11:24:46Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
<br />
My protein could have some<scene name='95/954099/Protein_view_2/1'> important future antibiotic use.</scene> <br />
== Biological relevance and broader implications ==<br />
<br />
== Important amino acids==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748384Sandbox Reserved 18022023-04-07T11:05:10Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
<br />
== Biological relevance and broader implications ==<br />
<br />
== Important amino acids==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Kevin Johnsonhttps://proteopedia.org/index.php?title=Sandbox_Reserved_1802&diff=3748383Sandbox Reserved 18022023-04-07T11:04:39Z<p>Kevin Johnson: </p>
<hr />
<div>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --><br />
==Your Heading Here (maybe something like 'Structure')==<br />
<StructureSection load='1802' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br />
<br />
== Function of your protein ==<br />
<br />
== Biological relevance and broader implications ==<br />
<br />
== Important amino acids==<br />
<br />
== Structural highlights ==<br />
<br />
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Kevin Johnson