5ess - Revision history

OCA at 12:29, 6 March 2024

2024-03-06T12:29:53Z

←Older revision		Revision as of 12:29, 6 March 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/MEND_MYCTU MEND_MYCTU] Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).		[https://www.uniprot.org/uniprot/MEND_MYCTU MEND_MYCTU] Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Menaquinone (MQ) is an essential component of the respiratory chains of many pathogenic organisms, including Mycobacterium tuberculosis (Mtb). The first committed step in MQ biosynthesis is catalyzed by 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD), a thiamin diphosphate (ThDP)-dependent enzyme. Catalysis proceeds through two covalent intermediates as the substrates 2-oxoglutarate and isochorismate are successively added to the cofactor before final cleavage of the product. We have determined a series of crystal structures of Mtb-MenD that map the binding of both substrates, visualizing each step in the MenD catalytic cycle, including both intermediates. ThDP binding induces a marked asymmetry between the coupled active sites of each dimer, and possible mechanisms of communication can be identified. The crystal structures also reveal conformational features of the two intermediates that facilitate reaction but prevent premature product release. These data fully map chemical space to inform early-stage drug discovery targeting MenD.
-
-	Structural Views along the Mycobacterium tuberculosis MenD Reaction Pathway Illuminate Key Aspects of Thiamin Diphosphate-Dependent Enzyme Mechanisms.,Jirgis EN, Bashiri G, Bulloch EM, Johnston JM, Baker EN Structure. 2016 Jul 6;24(7):1167-77. doi: 10.1016/j.str.2016.04.018. Epub 2016, Jun 9. PMID:27291649<ref>PMID:27291649</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5ess" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:21, 12 July 2023

2023-07-12T08:21:25Z

←Older revision		Revision as of 08:21, 12 July 2023
Line 1:		Line 1:

	==Crystal Structure of M. tuberculosis MenD bound to Mg2+ and covalent intermediate I (a ThDP and decarboxylated 2-oxoglutarate adduct)==		==Crystal Structure of M. tuberculosis MenD bound to Mg2+ and covalent intermediate I (a ThDP and decarboxylated 2-oxoglutarate adduct)==
-	<StructureSection load='5ess' size='340' side='right' caption='[[5ess]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='5ess' size='340' side='right'caption='[[5ess]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5ess]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Myctu Myctu~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ESS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ESS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5ess]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ESS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ESS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TOG:4-[3-[(4-AZANYL-2-METHYL-PYRIMIDIN-5-YL)METHYL]-4-METHYL-5-[2-[OXIDANYL(PHOSPHONOOXY)PHOSPHORYL]OXYETHYL]-1,3-THIAZOL-3-IUM-2-YL]-4-OXIDANYL-BUTANOIC+ACID'>TOG</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.2Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5esu\|5esu]], [[5eso\|5eso]], [[5erx\|5erx]], [[5ery\|5ery]], [[5esd\|5esd]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TOG:4-[3-[(4-AZANYL-2-METHYL-PYRIMIDIN-5-YL)METHYL]-4-METHYL-5-[2-[OXIDANYL(PHOSPHONOOXY)PHOSPHORYL]OXYETHYL]-1,3-THIAZOL-3-IUM-2-YL]-4-OXIDANYL-BUTANOIC+ACID'>TOG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">menD, Rv0555 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ess FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ess OCA], [https://pdbe.org/5ess PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ess RCSB], [https://www.ebi.ac.uk/pdbsum/5ess PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ess ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid_synthase 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.9 2.2.1.9] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ess FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ess OCA], [~~http~~://pdbe.org/5ess PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5ess RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5ess PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5ess ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MEND_MYCTU MEND_MYCTU]] Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).	+	[https://www.uniprot.org/uniprot/MEND_MYCTU MEND_MYCTU] Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Myctu~~]]	+	[[Category: Mycobacterium tuberculosis H37Rv]]
-	[[Category: Baker~~, E N~~]]	+	[[Category: Baker EN]]
-	[[Category: Bashiri, G]]	+	[[Category: Bashiri G]]
-	[[Category: Bulloch~~, E M.M~~]]	+	[[Category: Bulloch EMM]]
-	[[Category: Jirgis~~, E N.M~~]]	+	[[Category: Jirgis ENM]]
-	[[Category: Johnston~~, J M]]~~	+	[[Category: Johnston JM]]
-	~~[[Category: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase]]~~	+
-	~~[[Category: Menaquinone biosynthesis]]~~	+
-	~~[[Category: Mend]]~~	+
-	~~[[Category: Pyruvate oxidase family]]~~	+
-	~~[[Category: Thiamin-diphosphate dependent enzyme]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 09:55, 22 November 2017

2017-11-22T09:55:33Z

←Older revision		Revision as of 09:55, 22 November 2017
Line 3:		Line 3:
	<StructureSection load='5ess' size='340' side='right' caption='[[5ess]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='5ess' size='340' side='right' caption='[[5ess]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5ess]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ESS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ESS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5ess]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ESS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ESS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TOG:4-[3-[(4-AZANYL-2-METHYL-PYRIMIDIN-5-YL)METHYL]-4-METHYL-5-[2-[OXIDANYL(PHOSPHONOOXY)PHOSPHORYL]OXYETHYL]-1,3-THIAZOL-3-IUM-2-YL]-4-OXIDANYL-BUTANOIC+ACID'>TOG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TOG:4-[3-[(4-AZANYL-2-METHYL-PYRIMIDIN-5-YL)METHYL]-4-METHYL-5-[2-[OXIDANYL(PHOSPHONOOXY)PHOSPHORYL]OXYETHYL]-1,3-THIAZOL-3-IUM-2-YL]-4-OXIDANYL-BUTANOIC+ACID'>TOG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5esu\|5esu]], [[5eso\|5eso]], [[5erx\|5erx]], [[5ery\|5ery]], [[5esd\|5esd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5esu\|5esu]], [[5eso\|5eso]], [[5erx\|5erx]], [[5ery\|5ery]], [[5esd\|5esd]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">menD, Rv0555 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid_synthase 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.9 2.2.1.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid_synthase 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.9 2.2.1.9] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ess FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ess OCA], [http://pdbe.org/5ess PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ess RCSB], [http://www.ebi.ac.uk/pdbsum/5ess PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ess ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ess FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ess OCA], [http://pdbe.org/5ess PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ess RCSB], [http://www.ebi.ac.uk/pdbsum/5ess PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ess ProSAT]</span></td></tr>
Line 25:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase]]		[[Category: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase]]
		+	[[Category: Myctu]]
	[[Category: Baker, E N]]		[[Category: Baker, E N]]
	[[Category: Bashiri, G]]		[[Category: Bashiri, G]]

OCA at 17:35, 12 July 2016

2016-07-12T17:35:05Z

←Older revision		Revision as of 17:35, 12 July 2016
Line 7:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5esu\|5esu]], [[5eso\|5eso]], [[5erx\|5erx]], [[5ery\|5ery]], [[5esd\|5esd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5esu\|5esu]], [[5eso\|5eso]], [[5erx\|5erx]], [[5ery\|5ery]], [[5esd\|5esd]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid_synthase 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.9 2.2.1.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid_synthase 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.9 2.2.1.9] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ess FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ess OCA], [http://pdbe.org/5ess PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ess RCSB], [http://www.ebi.ac.uk/pdbsum/5ess PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ess FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ess OCA], [http://pdbe.org/5ess PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ess RCSB], [http://www.ebi.ac.uk/pdbsum/5ess PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ess ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/MEND_MYCTU MEND_MYCTU]] Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).		[[http://www.uniprot.org/uniprot/MEND_MYCTU MEND_MYCTU]] Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Menaquinone (MQ) is an essential component of the respiratory chains of many pathogenic organisms, including Mycobacterium tuberculosis (Mtb). The first committed step in MQ biosynthesis is catalyzed by 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD), a thiamin diphosphate (ThDP)-dependent enzyme. Catalysis proceeds through two covalent intermediates as the substrates 2-oxoglutarate and isochorismate are successively added to the cofactor before final cleavage of the product. We have determined a series of crystal structures of Mtb-MenD that map the binding of both substrates, visualizing each step in the MenD catalytic cycle, including both intermediates. ThDP binding induces a marked asymmetry between the coupled active sites of each dimer, and possible mechanisms of communication can be identified. The crystal structures also reveal conformational features of the two intermediates that facilitate reaction but prevent premature product release. These data fully map chemical space to inform early-stage drug discovery targeting MenD.
		+
		+	Structural Views along the Mycobacterium tuberculosis MenD Reaction Pathway Illuminate Key Aspects of Thiamin Diphosphate-Dependent Enzyme Mechanisms.,Jirgis EN, Bashiri G, Bulloch EM, Johnston JM, Baker EN Structure. 2016 Jul 6;24(7):1167-77. doi: 10.1016/j.str.2016.04.018. Epub 2016, Jun 9. PMID:27291649<ref>PMID:27291649</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5ess" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 23:24, 23 June 2016

2016-06-23T23:24:59Z

←Older revision		Revision as of 23:24, 23 June 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5ess is ~~ON HOLD until Paper Publication~~	+	==Crystal Structure of M. tuberculosis MenD bound to Mg2+ and covalent intermediate I (a ThDP and decarboxylated 2-oxoglutarate adduct)==
-		+	<StructureSection load='5ess' size='340' side='right' caption='[[5ess]], [[Resolution\|resolution]] 2.20Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5ess]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ESS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ESS FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TOG:4-[3-[(4-AZANYL-2-METHYL-PYRIMIDIN-5-YL)METHYL]-4-METHYL-5-[2-[OXIDANYL(PHOSPHONOOXY)PHOSPHORYL]OXYETHYL]-1,3-THIAZOL-3-IUM-2-YL]-4-OXIDANYL-BUTANOIC+ACID'>TOG</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5esu\|5esu]], [[5eso\|5eso]], [[5erx\|5erx]], [[5ery\|5ery]], [[5esd\|5esd]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid_synthase 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.9 2.2.1.9] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ess FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ess OCA], [http://pdbe.org/5ess PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ess RCSB], [http://www.ebi.ac.uk/pdbsum/5ess PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MEND_MYCTU MEND_MYCTU]] Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
		+	__TOC__
		+	</StructureSection>
		+	[[Category: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase]]
		+	[[Category: Baker, E N]]
		+	[[Category: Bashiri, G]]
		+	[[Category: Bulloch, E M.M]]
		+	[[Category: Jirgis, E N.M]]
		+	[[Category: Johnston, J M]]
		+	[[Category: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase]]
		+	[[Category: Menaquinone biosynthesis]]
		+	[[Category: Mend]]
		+	[[Category: Pyruvate oxidase family]]
		+	[[Category: Thiamin-diphosphate dependent enzyme]]
		+	[[Category: Transferase]]

OCA at 12:34, 15 May 2016

2016-05-15T12:34:22Z

←Older revision		Revision as of 12:34, 15 May 2016
Line 3:		Line 3:
	The entry 5ess is ON HOLD until Paper Publication		The entry 5ess is ON HOLD until Paper Publication

-	Authors: ~~Johnston, J.M., Jirgis, E.N.M., Bashiri, G., Bulloch, E.M.M., Baker, E.N.~~	+	Authors:

	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Johnston, J.M]]
-	[[Category: Bashiri, G]]
-	[[Category: Jirgis, E.N.M]]
-	[[Category: Bulloch, E.M.M]]
-	[[Category: Baker, E.N]]

OCA at 12:13, 16 December 2015

2015-12-16T12:13:36Z

←Older revision		Revision as of 12:13, 16 December 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5ess is ON HOLD	+	The entry 5ess is ON HOLD until Paper Publication

	Authors: Johnston, J.M., Jirgis, E.N.M., Bashiri, G., Bulloch, E.M.M., Baker, E.N.		Authors: Johnston, J.M., Jirgis, E.N.M., Bashiri, G., Bulloch, E.M.M., Baker, E.N.

OCA: Protected "5ess" [edit=sysop:move=sysop]

2015-12-01T03:19:18Z

Protected "5ess" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:19, 1 December 2015

OCA: New page: '''Unreleased structure''' The entry 5ess is ON HOLD Authors: Johnston, J.M., Jirgis, E.N.M., Bashiri, G., Bulloch, E.M.M., Baker, E.N. Description: [[Category: Unreleased Structures]...

2015-12-01T03:19:17Z

New page: '''Unreleased structure''' The entry 5ess is ON HOLD Authors: Johnston, J.M., Jirgis, E.N.M., Bashiri, G., Bulloch, E.M.M., Baker, E.N. Description: [[Category: Unreleased Structures]...

New page

'''Unreleased structure'''

The entry 5ess is ON HOLD

Authors: Johnston, J.M., Jirgis, E.N.M., Bashiri, G., Bulloch, E.M.M., Baker, E.N.

Description:
[[Category: Unreleased Structures]]
[[Category: Johnston, J.M]]
[[Category: Bashiri, G]]
[[Category: Jirgis, E.N.M]]
[[Category: Bulloch, E.M.M]]
[[Category: Baker, E.N]]