4gll - Revision history

OCA at 15:50, 14 March 2024

OCA — Thu, 14 Mar 2024 15:50:08 GMT

←Older revision		Revision as of 15:50, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gll]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ef7 4ef7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GLL FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gll]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ef7 4ef7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GLL FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.5Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4gll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gll OCA], [https://pdbe.org/4gll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gll RCSB], [https://www.ebi.ac.uk/pdbsum/4gll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gll ProSAT]</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=4gll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gll OCA], [https://pdbe.org/4gll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gll RCSB], [https://www.ebi.ac.uk/pdbsum/4gll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gll ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/UXS1_HUMAN UXS1_HUMAN] Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.		[https://www.uniprot.org/uniprot/UXS1_HUMAN UXS1_HUMAN] Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Human UDP-alpha-d-xylose synthase (hUXS) is a member of the short-chain dehydrogenase/reductase family of nucleotide-sugar modifying enzymes. hUXS contains a bound NAD(+) cofactor that it recycles by first oxidizing UDP-alpha-d-glucuronic acid (UGA), and then reducing the UDP-alpha-d-4-keto-xylose (UX4O) to produce UDP-alpha-d-xylose (UDX). Despite the observation that purified hUXS contains a bound cofactor, it has been reported that exogenous NAD(+) will stimulate enzyme activity. Here we show that a small fraction of hUXS releases the NADH and UX4O intermediates as products during turnover. The resulting apoenzyme can be rescued by exogenous NAD(+), explaining the apparent stimulatory effect of added cofactor. The slow release of NADH and UX4O as side products by hUXS is reminiscent of the Escherichia coli UGA decarboxylase (ArnA), a related enzyme that produces NADH and UX4O as products. We report that ArnA can rebind NADH and UX4O to slowly make UDX. This means that both enzymes share the same catalytic machinery, but differ in the preferred final product. We present a bifurcated rate equation that explains how the substrate is shunted to the distinct final products. Using a new crystal structure of hUXS, we identify the structural elements of the shunt and propose that the local unfolding of the active site directs reactants toward the preferred products. Finally, we present evidence that the release of NADH and UX4O involves a cooperative conformational change that is conserved in both enzymes.
-
-	Human UDP-alpha-d-xylose Synthase and Escherichia coli ArnA Conserve a Conformational Shunt That Controls Whether Xylose or 4-Keto-Xylose Is Produced.,Polizzi SJ, Walsh RM Jr, Peeples WB, Lim JM, Wells L, Wood ZA Biochemistry. 2012 Nov 6;51(44):8844-55. doi: 10.1021/bi301135b. Epub 2012 Oct, 29. PMID:23072385<ref>PMID:23072385</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4gll" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:04, 26 October 2022

OCA — Wed, 26 Oct 2022 07:04:18 GMT

←Older revision		Revision as of 07:04, 26 October 2022
Line 3:		Line 3:
	<StructureSection load='4gll' size='340' side='right'caption='[[4gll]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4gll' size='340' side='right'caption='[[4gll]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gll]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ef7 4ef7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GLL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gll]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ef7 4ef7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GLL FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2b69\|2b69]]</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=4gll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gll OCA], [https://pdbe.org/4gll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gll RCSB], [https://www.ebi.ac.uk/pdbsum/4gll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gll ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UNQ2538/PRO6079, UXS, UXS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-glucuronate_decarboxylase UDP-glucuronate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.35 4.1.1.35] </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=4gll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gll OCA], [~~http~~://pdbe.org/4gll PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gll RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gll PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gll ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/UXS1_HUMAN UXS1_HUMAN]] Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.	+	[https://www.uniprot.org/uniprot/UXS1_HUMAN UXS1_HUMAN] Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: UDP-glucuronate decarboxylase]]~~	+	[[Category: Polizzi SJ]]
-	[[Category: Polizzi~~, S J~~]]	+	[[Category: Wood ZA]]
-	[[Category: Wood~~, Z A]]~~	+
-	~~[[Category: Decarboxylase]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Membrane]]~~	+
-	~~[[Category: Short-chain dehydrogenase/reductase~~]]	+

OCA at 11:55, 17 July 2019

OCA — Wed, 17 Jul 2019 11:55:08 GMT

←Older revision		Revision as of 11:55, 17 July 2019
Line 1:		Line 1:

	==Crystal structure of human UDP-xylose synthase.==		==Crystal structure of human UDP-xylose synthase.==
-	<StructureSection load='4gll' size='340' side='right' caption='[[4gll]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='4gll' size='340' side='right'caption='[[4gll]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gll]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ef7 4ef7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GLL FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gll]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ef7 4ef7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GLL FirstGlance]. <br>
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: UDP-glucuronate decarboxylase]]		[[Category: UDP-glucuronate decarboxylase]]
	[[Category: Polizzi, S J]]		[[Category: Polizzi, S J]]

OCA at 01:05, 5 August 2016

OCA — Fri, 05 Aug 2016 01:05:25 GMT

←Older revision		Revision as of 01:05, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of human UDP-xylose synthase.==		==Crystal structure of human UDP-xylose synthase.==
	<StructureSection load='4gll' size='340' side='right' caption='[[4gll]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4gll' size='340' side='right' caption='[[4gll]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gll]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ef7 4ef7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GLL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gll]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ef7 4ef7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GLL FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2b69\|2b69]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2b69\|2b69]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UNQ2538/PRO6079, UXS, UXS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UNQ2538/PRO6079, UXS, UXS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-glucuronate_decarboxylase UDP-glucuronate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.35 4.1.1.35] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-glucuronate_decarboxylase UDP-glucuronate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.35 4.1.1.35] </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=4gll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gll OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gll RCSB], [http://www.ebi.ac.uk/pdbsum/4gll 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=4gll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gll OCA], [http://pdbe.org/4gll PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gll RCSB], [http://www.ebi.ac.uk/pdbsum/4gll PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gll ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4gll" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: UDP-glucuronate decarboxylase]]		[[Category: UDP-glucuronate decarboxylase]]
	[[Category: Polizzi, S J]]		[[Category: Polizzi, S J]]

OCA at 14:34, 25 December 2014

OCA — Thu, 25 Dec 2014 14:34:32 GMT

←Older revision		Revision as of 14:34, 25 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4gll.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of human UDP-xylose synthase.==
		+	<StructureSection load='4gll' size='340' side='right' caption='[[4gll]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4gll]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ef7 4ef7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GLL FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2b69\|2b69]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UNQ2538/PRO6079, UXS, UXS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-glucuronate_decarboxylase UDP-glucuronate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.35 4.1.1.35] </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=4gll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gll OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gll RCSB], [http://www.ebi.ac.uk/pdbsum/4gll PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/UXS1_HUMAN UXS1_HUMAN]] Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human UDP-alpha-d-xylose synthase (hUXS) is a member of the short-chain dehydrogenase/reductase family of nucleotide-sugar modifying enzymes. hUXS contains a bound NAD(+) cofactor that it recycles by first oxidizing UDP-alpha-d-glucuronic acid (UGA), and then reducing the UDP-alpha-d-4-keto-xylose (UX4O) to produce UDP-alpha-d-xylose (UDX). Despite the observation that purified hUXS contains a bound cofactor, it has been reported that exogenous NAD(+) will stimulate enzyme activity. Here we show that a small fraction of hUXS releases the NADH and UX4O intermediates as products during turnover. The resulting apoenzyme can be rescued by exogenous NAD(+), explaining the apparent stimulatory effect of added cofactor. The slow release of NADH and UX4O as side products by hUXS is reminiscent of the Escherichia coli UGA decarboxylase (ArnA), a related enzyme that produces NADH and UX4O as products. We report that ArnA can rebind NADH and UX4O to slowly make UDX. This means that both enzymes share the same catalytic machinery, but differ in the preferred final product. We present a bifurcated rate equation that explains how the substrate is shunted to the distinct final products. Using a new crystal structure of hUXS, we identify the structural elements of the shunt and propose that the local unfolding of the active site directs reactants toward the preferred products. Finally, we present evidence that the release of NADH and UX4O involves a cooperative conformational change that is conserved in both enzymes.

-	~~{{STRUCTURE_4gll\| PDB=4gll \| SCENE= }}~~	+	Human UDP-alpha-d-xylose Synthase and Escherichia coli ArnA Conserve a Conformational Shunt That Controls Whether Xylose or 4-Keto-Xylose Is Produced.,Polizzi SJ, Walsh RM Jr, Peeples WB, Lim JM, Wells L, Wood ZA Biochemistry. 2012 Nov 6;51(44):8844-55. doi: 10.1021/bi301135b. Epub 2012 Oct, 29. PMID:23072385<ref>PMID:23072385</ref>

-	~~===Crystal structure~~ of ~~human UDP-xylose synthase~~.~~===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	==~~About this Structure~~==	+	<references/>
-	~~[[4gll]] is a 2 chain structure with sequence from [http:~~//en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ef7 4ef7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLL OCA].	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: UDP-glucuronate decarboxylase]]		[[Category: UDP-glucuronate decarboxylase]]
-	[[Category: Polizzi, S J.]]	+	[[Category: Polizzi, S J]]
-	[[Category: Wood, Z A.]]	+	[[Category: Wood, Z A]]
	[[Category: Decarboxylase]]		[[Category: Decarboxylase]]
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Membrane]]		[[Category: Membrane]]
	[[Category: Short-chain dehydrogenase/reductase]]		[[Category: Short-chain dehydrogenase/reductase]]

OCA at 06:45, 14 November 2012

OCA — Wed, 14 Nov 2012 06:45:42 GMT

←Older revision		Revision as of 06:45, 14 November 2012
Line 1:		Line 1:
-	[[Image:4gll.~~jpg~~\|left\|200px]]	+	[[Image:4gll.png\|left\|200px]]

	{{STRUCTURE_4gll\| PDB=4gll \| SCENE= }}		{{STRUCTURE_4gll\| PDB=4gll \| SCENE= }}

OCA at 05:15, 5 September 2012

OCA — Wed, 05 Sep 2012 05:15:01 GMT

←Older revision		Revision as of 05:15, 5 September 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4gll.jpg\|left\|200px]]

-	~~The entry~~ 4gll ~~is ON HOLD~~	+	{{STRUCTURE_4gll\| PDB=4gll \| SCENE= }}

-	~~Authors: Wood, Z.A., Polizzi, S.J~~.	+	===Crystal structure of human UDP-xylose synthase.===

-	~~Description~~: ~~Crystal~~ structure ~~of human~~ UDP-~~xylose synthase~~.	+
		+	==About this Structure==
		+	[[4gll]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ef7 4ef7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLL OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: UDP-glucuronate decarboxylase]]
		+	[[Category: Polizzi, S J.]]
		+	[[Category: Wood, Z A.]]
		+	[[Category: Decarboxylase]]
		+	[[Category: Lyase]]
		+	[[Category: Membrane]]
		+	[[Category: Short-chain dehydrogenase/reductase]]

OCA: Protected "4gll" [edit=sysop:move=sysop]

OCA — Wed, 22 Aug 2012 05:36:57 GMT

Protected "4gll" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:36, 22 August 2012

OCA: New page: '''Unreleased structure''' The entry 4gll is ON HOLD Authors: Wood, Z.A., Polizzi, S.J. Description: Crystal structure of human UDP-xylose synthase.

OCA — Wed, 22 Aug 2012 05:36:56 GMT

New page: '''Unreleased structure''' The entry 4gll is ON HOLD Authors: Wood, Z.A., Polizzi, S.J. Description: Crystal structure of human UDP-xylose synthase.

New page

'''Unreleased structure'''

The entry 4gll is ON HOLD

Authors: Wood, Z.A., Polizzi, S.J.

Description: Crystal structure of human UDP-xylose synthase.