5lqs - Revision history

OCA at 18:41, 18 October 2023

OCA — Wed, 18 Oct 2023 18:41:49 GMT

←Older revision		Revision as of 18:41, 18 October 2023
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	<StructureSection load='5lqs' size='340' side='right'caption='[[5lqs]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='5lqs' size='340' side='right'caption='[[5lqs]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lqs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LQS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5LQS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lqs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LQS FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>~~, ~~<scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 1.9Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[4p3x\|4p3x]]~~<~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/Quinolinate_synthase Quinolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.72 2.5.1.72]~~ </~~span~~></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=5lqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lqs OCA], [https://pdbe.org/5lqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lqs RCSB], [https://www.ebi.ac.uk/pdbsum/5lqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lqs ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5lqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lqs OCA], [~~http~~://pdbe.org/5lqs PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5lqs RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5lqs PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5lqs ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/NADA_THEMA NADA_THEMA]] Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity).	+	[https://www.uniprot.org/uniprot/NADA_THEMA NADA_THEMA] Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Quinolinate synthase~~]]	+	[[Category: Thermotoga maritima MSB8]]
-	[[Category: Fontecilla-Camps~~, J C~~]]	+	[[Category: Fontecilla-Camps JC]]
-	[[Category: Volbeda, A]]	+	[[Category: Volbeda A]]
-	~~[[Category: Iron sulfur cluster]]~~	+
-	~~[[Category: Nad biosynthesis]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 10:47, 12 August 2020

OCA — Wed, 12 Aug 2020 10:47:19 GMT

←Older revision		Revision as of 10:47, 12 August 2020
Line 1:		Line 1:

	==Structure of quinolinate synthase Y21F mutant in complex with substrate-derived quinolinate==		==Structure of quinolinate synthase Y21F mutant in complex with substrate-derived quinolinate==
-	<StructureSection load='5lqs' size='340' side='right' caption='[[5lqs]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='5lqs' size='340' side='right'caption='[[5lqs]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lqs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LQS OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5LQS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lqs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LQS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LQS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4p3x\|4p3x]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4p3x\|4p3x]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Quinolinate_synthase Quinolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.72 2.5.1.72] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Quinolinate_synthase Quinolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.72 2.5.1.72] </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=5lqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lqs OCA], [http://pdbe.org/5lqs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lqs RCSB], [http://www.ebi.ac.uk/pdbsum/5lqs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lqs ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lqs OCA], [http://pdbe.org/5lqs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lqs RCSB], [http://www.ebi.ac.uk/pdbsum/5lqs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lqs ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Quinolinate synthase]]		[[Category: Quinolinate synthase]]
	[[Category: Fontecilla-Camps, J C]]		[[Category: Fontecilla-Camps, J C]]

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

OCA — Fri, 09 Sep 2016 05:34:39 GMT

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

←Older revision

Revision as of 05:34, 9 September 2016

OCA: New page: ==Structure of quinolinate synthase Y21F mutant in complex with substrate-derived quinolinate== == Structural highlights ==
<table><tr><td colspan='2'>[[5lqs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LQS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LQS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p3x|4p3x]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Quinolinate_synthase Quinolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.72 2.5.1.72] </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=5lqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lqs OCA], [http://pdbe.org/5lqs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lqs RCSB], [http://www.ebi.ac.uk/pdbsum/5lqs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lqs ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/NADA_THEMA NADA_THEMA]] Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The enzyme NadA catalyzes the synthesis of quinolinic acid (QA), the precursor of the universal nicotinamide adenine dinucleotide (NAD) cofactor. Here, we report the crystal structures of complexes between the Thermotoga maritima (Tm) NadA K219R/Y107F variant and (i) the first intermediate (W) resulting from the condensation of dihydroxyacetone phosphate (DHAP) with iminoaspartate and (ii) the DHAP analogue and triose-phosphate isomerase inhibitor phosphoglycolohydroxamate (PGH). In addition, using the TmNadA K219R/Y21F variant, we have reacted substrates and obtained a crystalline complex between this protein and the QA product. We also show that citrate can bind to both TmNadA K219R and its Y21F variant. The W structure indicates that condensation causes dephosphorylation. We propose that catalysis by the K219R/Y107F variant is arrested at the W intermediate because the mutated protein is unable to catalyze its aldo-keto isomerization and/or cyclization that ultimately lead to QA formation. Intriguingly, PGH binds to NadA with its phosphate group at the site where the carboxylate groups of W also bind. Our results shed significant light on the mechanism of the reaction catalyzed by NadA.

Crystal Structures of Quinolinate Synthase in Complex with a Substrate Analogue, the Condensation Intermediate, and Substrate-Derived Product.,Volbeda A, Darnault C, Renoux O, Reichmann D, Amara P, Ollagnier de Choudens S, Fontecilla-Camps JC J Am Chem Soc. 2016 Aug 30. PMID:27545412<ref>PMID:27545412</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lqs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
TOC
</StructureSection>
[[Category: Quinolinate synthase]]
[[Category: Fontecilla-Camps, J C]]
[[Category: Volbeda, A]]
[[Category: Iron sulfur cluster]]
[[Category: Nad biosynthesis]]
[[Category: Transferase]]