Chorismate mutase - Revision history

Alexander Berchansky at 15:40, 10 July 2022

Alexander Berchansky — Sun, 10 Jul 2022 15:40:19 GMT

←Older revision		Revision as of 15:40, 10 July 2022
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	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The <scene name='91/916399/Cv/4'>transition state analog is buried in the active site pocket and forms extensive H-bond network</scene> with CHM. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. Overlaying the structure of the unliganded CHM with that of the complex ~~shos~~ a movement of the second shell residues Arg 72 and Gln 75 which can allow the entry of the transition state analog to the active site pocket.	+	The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The <scene name='91/916399/Cv/4'>transition state analog is buried in the active site pocket and forms extensive H-bond network</scene> with CHM. Water molecule is shown as red sphere. <scene name='91/916399/Cv/5'>Arg 49 and Arg 134</scene> (in magenra) which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. Overlaying the structure of the unliganded CHM with that of the complex shoes a movement of the <scene name='91/916399/Cv/6'>second shell residues Arg 72 and Gln 75</scene> (in lavender) which can allow the entry of the transition state analog to the active site pocket.

	==Chorismate mutase 3D structures==		==Chorismate mutase 3D structures==

Alexander Berchansky at 15:33, 10 July 2022

Alexander Berchansky — Sun, 10 Jul 2022 15:33:03 GMT

←Older revision		Revision as of 15:33, 10 July 2022
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	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The transition state analog is buried in the active site pocket and forms extensive H-bond network with CHM. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. Overlaying the structure of the unliganded CHM with that of the complex shos a movement of the second shell residues Arg 72 and Gln 75 which can allow the entry of the transition state analog to the active site pocket. ~~<scene name='91/916399/Cv/2'>TextToBeDisplayed</scene>~~	+	The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The <scene name='91/916399/Cv/4'>transition state analog is buried in the active site pocket and forms extensive H-bond network</scene> with CHM. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. Overlaying the structure of the unliganded CHM with that of the complex shos a movement of the second shell residues Arg 72 and Gln 75 which can allow the entry of the transition state analog to the active site pocket.

	==Chorismate mutase 3D structures==		==Chorismate mutase 3D structures==

Alexander Berchansky at 11:52, 10 July 2022

Alexander Berchansky — Sun, 10 Jul 2022 11:52:04 GMT

←Older revision		Revision as of 11:52, 10 July 2022
Line 11:		Line 11:
	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The transition state analog is buried in the active site pocket and forms extensive H-bond network with CHM. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. Overlaying the structure of the unliganded CHM with that of the complex shos a movement of the second shell residues Arg 72 and Gln 75 which can allow the entry of the transition state analog to the active site pocket.	+	The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The transition state analog is buried in the active site pocket and forms extensive H-bond network with CHM. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. Overlaying the structure of the unliganded CHM with that of the complex shos a movement of the second shell residues Arg 72 and Gln 75 which can allow the entry of the transition state analog to the active site pocket. <scene name='91/916399/Cv/2'>TextToBeDisplayed</scene>

	==Chorismate mutase 3D structures==		==Chorismate mutase 3D structures==

Alexander Berchansky at 11:43, 10 July 2022

Alexander Berchansky — Sun, 10 Jul 2022 11:43:31 GMT

←Older revision		Revision as of 11:43, 10 July 2022
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-	<StructureSection load='2fp2' size='340' side='right' caption='Bacillus subtilis chorismate mutase complex with transition state analog (PDB code [[2fp2]]).' scene=''>	+	<StructureSection load='2fp2' size='340' side='right' caption='Bacillus subtilis chorismate mutase complex with transition state analog (PDB code [[2fp2]]).' scene='91/916399/Cv/1'>

	== Function ==		== Function ==

Alexander Berchansky at 11:40, 10 July 2022

Alexander Berchansky — Sun, 10 Jul 2022 11:40:51 GMT

←Older revision		Revision as of 11:40, 10 July 2022
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	== Function ==		== Function ==

-	'''Chorismate mutase'''.(CHM) is a key enzyme in the biosynthesis of aromatic amino acids Phe and Tyr . CHM catalyzes the rearrangement of chorismate to prephenate which is the precursor of Phe and Tyr<ref>PMID:21638687</ref>.. CHM is divided ןמto 2 classes: AroH class which is monofunctional and thק bifunctional AroQ.	+	'''Chorismate mutase''' (CHM) is a key enzyme in the biosynthesis of aromatic amino acids Phe and Tyr. CHM catalyzes the rearrangement of chorismate to prephenate which is the precursor of Phe and Tyr<ref>PMID:21638687</ref>. CHM is divided ןמto 2 classes: AroH class which is monofunctional and thק bifunctional AroQ.

	== Relevance ==		== Relevance ==

-	CHM belongs to the aromatic acids biogenesis pathway in prokaryotes which differs from that of humans. Hence, the presence of CHM indicates the presence of virulent bacteria and its detection is used in developing rational therapeutics against bacterial virulence<ref>PMID:29717997</ref>.	+	CHM belongs to the aromatic acids biogenesis pathway in prokaryotes which differs from that of humans. Hence, the presence of CHM indicates the presence of virulent bacteria and its detection is used in developing rational therapeutics against bacterial virulence<ref>PMID:29717997</ref>.

	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The transition state analog is buried in the active site pocket and forms extensive H-bond network with CHM. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. Overlaying the structure of the unliganded CHM with that of the complex shos a movement of the second shell residues Arg 72 and Gln 75 which can allow the entry of the transition state analog to the active site pocket.	+	The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The transition state analog is buried in the active site pocket and forms extensive H-bond network with CHM. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. Overlaying the structure of the unliganded CHM with that of the complex shos a movement of the second shell residues Arg 72 and Gln 75 which can allow the entry of the transition state analog to the active site pocket.

	==Chorismate mutase 3D structures==		==Chorismate mutase 3D structures==

Michal Harel at 07:43, 6 July 2022

Michal Harel — Wed, 06 Jul 2022 07:43:48 GMT

←Older revision		Revision as of 07:43, 6 July 2022
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	'''Chorismate mutase'''.(CHM) is a key enzyme in the biosynthesis of aromatic amino acids Phe and Tyr . CHM catalyzes the rearrangement of chorismate to prephenate which is the precursor of Phe and Tyr<ref>PMID:21638687</ref>.. CHM is divided ןמto 2 classes: AroH class which is monofunctional and thק bifunctional AroQ.		'''Chorismate mutase'''.(CHM) is a key enzyme in the biosynthesis of aromatic amino acids Phe and Tyr . CHM catalyzes the rearrangement of chorismate to prephenate which is the precursor of Phe and Tyr<ref>PMID:21638687</ref>.. CHM is divided ןמto 2 classes: AroH class which is monofunctional and thק bifunctional AroQ.
-
-	== Disease ==

	== Relevance ==		== Relevance ==
		+
		+	CHM belongs to the aromatic acids biogenesis pathway in prokaryotes which differs from that of humans. Hence, the presence of CHM indicates the presence of virulent bacteria and its detection is used in developing rational therapeutics against bacterial virulence<ref>PMID:29717997</ref>.

	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The transition state analog is buried in the active site pocket and forms extensive H-bond network with CHM. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>.	+	The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The transition state analog is buried in the active site pocket and forms extensive H-bond network with CHM. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>. Overlaying the structure of the unliganded CHM with that of the complex shos a movement of the second shell residues Arg 72 and Gln 75 which can allow the entry of the transition state analog to the active site pocket.
		+
		+	==Chorismate mutase 3D structures==
		+
		+	[[3D structures of chorismate mutase]]

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Michal Harel at 07:26, 6 July 2022

Michal Harel — Wed, 06 Jul 2022 07:26:53 GMT

←Older revision		Revision as of 07:26, 6 July 2022
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-	<StructureSection load='~~4ppv~~' size='340' side='right' caption='Bacillus subtilis chorismate mutase complex with ~~chorismate, prephenate and citrulline~~ (PDB code [[~~3zp7~~]]).' scene=''>	+	<StructureSection load='2fp2' size='340' side='right' caption='Bacillus subtilis chorismate mutase complex with transition state analog (PDB code [[2fp2]]).' scene=''>

	== Function ==		== Function ==

-	'''Chorismate mutase'''.(CHM) is a key enzyme in the biosynthesis of aromatic amino acids Phe and Tyr . CHM catalyzes the rearrangement of chorismate to prephenate which is the precursor of Phe and Tyr<ref>PMID:21638687</ref>.. CHM is divided to 2 classes: AroH class which is monofunctional and th bifunctional AroQ.	+	'''Chorismate mutase'''.(CHM) is a key enzyme in the biosynthesis of aromatic amino acids Phe and Tyr . CHM catalyzes the rearrangement of chorismate to prephenate which is the precursor of Phe and Tyr<ref>PMID:21638687</ref>.. CHM is divided ןמto 2 classes: AroH class which is monofunctional and thק bifunctional AroQ.

	== Disease ==		== Disease ==
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	== Structural highlights ==		== Structural highlights ==

-	~~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~~.	+	The 3D structure of the complex of CHM with transition state analog shows the CHM structure containing a dimer of pseudosymmetry but only the N-terminal half contains an available active site pocket. The transition state analog is buried in the active site pocket and forms extensive H-bond network with CHM. Arg 49 and Arg 134 which are part of this network are conserved in all the known CHMs<ref>PMID:16499927</ref>.

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Michal Harel at 09:41, 5 July 2022

Michal Harel — Tue, 05 Jul 2022 09:41:26 GMT

←Older revision		Revision as of 09:41, 5 July 2022
Line 1:		Line 1:
-	<StructureSection load='~~3zp7~~' size='340' side='right' caption='Bacillus subtilis chorismate mutase complex with chorismate, prephenate and citrulline (PDB code [[3zp7]]).' scene=''>	+	<StructureSection load='4ppv' size='340' side='right' caption='Bacillus subtilis chorismate mutase complex with chorismate, prephenate and citrulline (PDB code [[3zp7]]).' scene=''>

	== Function ==		== Function ==

Michal Harel at 08:26, 5 July 2022

Michal Harel — Tue, 05 Jul 2022 08:26:24 GMT

←Older revision		Revision as of 08:26, 5 July 2022
Line 1:		Line 1:
-	<StructureSection load='3zp7' size='340' side='right' caption='~~Caption for this structure~~' scene=''>	+	<StructureSection load='3zp7' size='340' side='right' caption='Bacillus subtilis chorismate mutase complex with chorismate, prephenate and citrulline (PDB code [[3zp7]]).' scene=''>

	== Function ==		== Function ==

Michal Harel at 08:23, 5 July 2022

Michal Harel — Tue, 05 Jul 2022 08:23:52 GMT

←Older revision		Revision as of 08:23, 5 July 2022
Line 1:		Line 1:
-		+	<StructureSection load='3zp7' size='340' side='right' caption='Caption for this structure' scene=''>
-	<StructureSection load='~~1stp~~' size='340' side='right' caption='Caption for this structure' scene=''>	+

	== Function ==		== Function ==