Sandbox Reserved 1802: Difference between revisions

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{{Sandbox_Reserved_CHEM351_Spring2023}}

<scene name='95/954099/Hydrogen_bonds/4'>Text To Be Displayed</scene>{{Sandbox_Reserved_CHEM351_Spring2023}}

== Chorismate dehydratase (MqnA) ==

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== Function of your protein ==

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).

== Biological relevance and broader implications ==

~~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.

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.

== Important amino acids==

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>.

~~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>~~

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>

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>

ISJ (A) has the following Hydrophobic interaction with ScMqnA: <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene>

ISJ (B) has the following Hydrogen bonds with ScMqnA: ~~THR59~~, ~~SER86~~, ~~SER109~~, ~~ARG110~~, ~~SER112~~, ~~GLY151~~, ~~PHE186~~, ~~PHE243~~

ISJ (B) has the following Hydrogen bonds with ScMqnA: THR60, SER87, CYS88, SER110, ARG111, THR112, SER113, GLY152, PHE187, THR243

ISJ (B) has the following Hydrophobic interaction with ScMqnA: ~~PRO41~~, ~~VAL78~~, ~~VAL84~~, ~~ILE150~~, ~~PHE186~~

ISJ (B) has the following Hydrophobic interaction with ScMqnA: PRO42, VAL79, VAL85, ILE151, PHE187

== Structural highlights ==

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.

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.

== Other Important Features ==

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-{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
+<scene name='95/954099/Hydrogen_bonds/4'>Text To Be Displayed</scene>{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
 == Chorismate dehydratase (MqnA) ==
 <StructureSection load='7AN6' size='340' side='right' caption='Caption for this structure' scene=''>
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 == Function of your protein ==
 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).
 == Biological relevance and broader implications ==
-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.
+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.
 == Important amino acids==
+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>.
-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>
+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>
-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>
 ISJ (A) has the following Hydrophobic interaction with ScMqnA:     <scene name='95/954099/Hydrophobic/3'>PRO42, VAL79, VAL85, PHE186, TYR243</scene>
-ISJ (B) has the following Hydrogen bonds with ScMqnA:                 THR59, SER86, SER109, ARG110, SER112, GLY151, PHE186, PHE243
+ISJ (B) has the following Hydrogen bonds with ScMqnA:                 THR60, SER87, CYS88, SER110, ARG111, THR112, SER113, GLY152, PHE187, THR243
-ISJ (B) has the following Hydrophobic interaction with ScMqnA:     PRO41, VAL78, VAL84, ILE150, PHE186
+ISJ (B) has the following Hydrophobic interaction with ScMqnA:     PRO42, VAL79, VAL85, ILE151, PHE187
 == Structural highlights ==
-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.
+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.
 == Other Important Features ==