4m55 - Revision history

OCA at 12:24, 1 March 2024

OCA — Fri, 01 Mar 2024 12:24:11 GMT

←Older revision		Revision as of 12:24, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4m55]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M55 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4m55]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M55 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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]] 2.86Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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=4m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m55 OCA], [https://pdbe.org/4m55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m55 RCSB], [https://www.ebi.ac.uk/pdbsum/4m55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m55 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=4m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m55 OCA], [https://pdbe.org/4m55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m55 RCSB], [https://www.ebi.ac.uk/pdbsum/4m55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m55 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 ==
-	The man o' war (mow) phenotype in zebrafish is characterized by severe craniofacial defects due to a missense mutation in UDP-alpha-d-xylose synthase (UXS), an essential enzyme in proteoglycan biosynthesis. The mow mutation is located in the UXS dimer interface approximately 16 A away from the active site, suggesting an indirect effect on the enzyme mechanism. We have examined the structural and catalytic consequences of the mow mutation (R236H) in the soluble fragment of human UXS (hUXS), which shares 93% sequence identity with the zebrafish enzyme. In solution, hUXS dimers undergo a concentration-dependent association to form a tetramer. Sedimentation velocity studies show that the R236H substitution induces the formation of a new hexameric species. Using two new crystal structures of the hexamer, we show that R236H and R236A substitutions cause a local unfolding of the active site that allows for a rotation of the dimer interface necessary to form the hexamer. The disordered active sites in the R236H and R236A mutant constructs displace Y231, the essential acid/base catalyst in the UXS reaction mechanism. The loss of Y231 favors an abortive catalytic cycle in which the reaction intermediate, UDP-alpha-d-4-keto-xylose, is not reduced to the final product, UDP-alpha-d-xylose. Surprisingly, the mow-induced hexamer is almost identical to the hexamers formed by the deeply divergent UXS homologues from Staphylococcus aureus and Helicobacter pylori (21% and 16% sequence identity, respectively). The persistence of a latent hexamer-building interface in the human enzyme suggests that the ancestral UXS may have been a hexamer.
-
-	Man o' war mutation in UDP-alpha-D-xylose synthase favors the abortive catalytic cycle and uncovers a latent potential for hexamer formation.,Walsh RM Jr, Polizzi SJ, Kadirvelraj R, Howard WW, Wood ZA Biochemistry. 2015 Jan 27;54(3):807-19. doi: 10.1021/bi501357c. Epub 2015 Jan 13. PMID:25521717<ref>PMID:25521717</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4m55" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:56, 21 December 2022

OCA — Wed, 21 Dec 2022 10:56:39 GMT

←Older revision		Revision as of 10:56, 21 December 2022
Line 1:		Line 1:

	==Crystal structure of Human UDP-xylose synthase R236H substitution==		==Crystal structure of Human UDP-xylose synthase R236H substitution==
-	<StructureSection load='4m55' size='340' side='right' caption='[[4m55]], [[Resolution\|resolution]] 2.86Å' scene=''>	+	<StructureSection load='4m55' size='340' side='right'caption='[[4m55]], [[Resolution\|resolution]] 2.86Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4m55]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M55 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4M55 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4m55]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M55 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lk3\|4lk3]]</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=4m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m55 OCA], [https://pdbe.org/4m55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m55 RCSB], [https://www.ebi.ac.uk/pdbsum/4m55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m55 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=4m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m55 OCA], [~~http~~://pdbe.org/4m55 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4m55 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4m55 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4m55 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: ~~UDP-glucuronate decarboxylase~~]]	+	[[Category: Large Structures]]
-	[[Category: Polizzi~~, S J~~]]	+	[[Category: Polizzi SJ]]
-	[[Category: Walsh~~, R M~~]]	+	[[Category: Walsh Jr RM]]
-	[[Category: Wood~~, Z A]]~~	+	[[Category: Wood ZA]]
-	~~[[Category: Decarboxylase]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Membrane]]~~	+
-	~~[[Category: Rossmann fold]]~~	+
-	~~[[Category: Short-chain dehydrogenase/reductase~~]]	+

OCA at 17:28, 9 March 2017

OCA — Thu, 09 Mar 2017 17:28:41 GMT

←Older revision		Revision as of 17:28, 9 March 2017
Line 1:		Line 1:
		+
	==Crystal structure of Human UDP-xylose synthase R236H substitution==		==Crystal structure of Human UDP-xylose synthase R236H substitution==
	<StructureSection load='4m55' size='340' side='right' caption='[[4m55]], [[Resolution\|resolution]] 2.86Å' scene=''>		<StructureSection load='4m55' size='340' side='right' caption='[[4m55]], [[Resolution\|resolution]] 2.86Å' scene=''>
Line 7:		Line 8:
	<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='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=4m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m55 RCSB], [http://www.ebi.ac.uk/pdbsum/4m55 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=4m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m55 OCA], [http://pdbe.org/4m55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m55 RCSB], [http://www.ebi.ac.uk/pdbsum/4m55 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m55 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 4m55" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:03, 3 June 2015

OCA — Wed, 03 Jun 2015 07:03:24 GMT

←Older revision		Revision as of 07:03, 3 June 2015
Line 11:		Line 11:
	== 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.		[[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 ==
		+	The man o' war (mow) phenotype in zebrafish is characterized by severe craniofacial defects due to a missense mutation in UDP-alpha-d-xylose synthase (UXS), an essential enzyme in proteoglycan biosynthesis. The mow mutation is located in the UXS dimer interface approximately 16 A away from the active site, suggesting an indirect effect on the enzyme mechanism. We have examined the structural and catalytic consequences of the mow mutation (R236H) in the soluble fragment of human UXS (hUXS), which shares 93% sequence identity with the zebrafish enzyme. In solution, hUXS dimers undergo a concentration-dependent association to form a tetramer. Sedimentation velocity studies show that the R236H substitution induces the formation of a new hexameric species. Using two new crystal structures of the hexamer, we show that R236H and R236A substitutions cause a local unfolding of the active site that allows for a rotation of the dimer interface necessary to form the hexamer. The disordered active sites in the R236H and R236A mutant constructs displace Y231, the essential acid/base catalyst in the UXS reaction mechanism. The loss of Y231 favors an abortive catalytic cycle in which the reaction intermediate, UDP-alpha-d-4-keto-xylose, is not reduced to the final product, UDP-alpha-d-xylose. Surprisingly, the mow-induced hexamer is almost identical to the hexamers formed by the deeply divergent UXS homologues from Staphylococcus aureus and Helicobacter pylori (21% and 16% sequence identity, respectively). The persistence of a latent hexamer-building interface in the human enzyme suggests that the ancestral UXS may have been a hexamer.
		+
		+	Man o' war mutation in UDP-alpha-D-xylose synthase favors the abortive catalytic cycle and uncovers a latent potential for hexamer formation.,Walsh RM Jr, Polizzi SJ, Kadirvelraj R, Howard WW, Wood ZA Biochemistry. 2015 Jan 27;54(3):807-19. doi: 10.1021/bi501357c. Epub 2015 Jan 13. PMID:25521717<ref>PMID:25521717</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 18:40, 25 December 2014

OCA — Thu, 25 Dec 2014 18:40:08 GMT

←Older revision		Revision as of 18:40, 25 December 2014
Line 2:		Line 2:
	<StructureSection load='4m55' size='340' side='right' caption='[[4m55]], [[Resolution\|resolution]] 2.86Å' scene=''>		<StructureSection load='4m55' size='340' side='right' caption='[[4m55]], [[Resolution\|resolution]] 2.86Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4m55]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M55 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4m55]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M55 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lk3\|4lk3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lk3\|4lk3]]</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=4m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m55 RCSB], [http://www.ebi.ac.uk/pdbsum/4m55 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=4m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m55 RCSB], [http://www.ebi.ac.uk/pdbsum/4m55 PDBsum]</span></td></tr>
	</table>		</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.
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: UDP-glucuronate decarboxylase]]		[[Category: UDP-glucuronate decarboxylase]]
	[[Category: Polizzi, S J]]		[[Category: Polizzi, S J]]

OCA at 07:38, 12 November 2014

OCA — Wed, 12 Nov 2014 07:38:50 GMT

←Older revision		Revision as of 07:38, 12 November 2014
Line 2:		Line 2:
	<StructureSection load='4m55' size='340' side='right' caption='[[4m55]], [[Resolution\|resolution]] 2.86Å' scene=''>		<StructureSection load='4m55' size='340' side='right' caption='[[4m55]], [[Resolution\|resolution]] 2.86Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4m55]] is a 6 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M55 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4m55]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M55 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lk3\|4lk3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lk3\|4lk3]]</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='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=4m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m55 RCSB], [http://www.ebi.ac.uk/pdbsum/4m55 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=4m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m55 RCSB], [http://www.ebi.ac.uk/pdbsum/4m55 PDBsum]</span></td></tr>
Line 11:		Line 10:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Homo sapiens]]
	[[Category: UDP-glucuronate decarboxylase]]		[[Category: UDP-glucuronate decarboxylase]]
-	[[Category: Polizzi, S J.]]	+	[[Category: Polizzi, S J]]
-	[[Category: Walsh, R M.]]	+	[[Category: Walsh, R M]]
-	[[Category: Wood, Z A.]]	+	[[Category: Wood, Z A]]
	[[Category: Decarboxylase]]		[[Category: Decarboxylase]]
	[[Category: Lyase]]		[[Category: Lyase]]

OCA at 14:08, 3 November 2014

OCA — Mon, 03 Nov 2014 14:08:34 GMT

←Older revision		Revision as of 14:08, 3 November 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4m55\| PDB=4m55 \| SCENE= }}~~	+	==Crystal structure of Human UDP-xylose synthase R236H substitution==
-	===Crystal structure of Human UDP-xylose synthase R236H substitution===	+	<StructureSection load='4m55' size='340' side='right' caption='[[4m55]], [[Resolution\|resolution]] 2.86Å' scene=''>
-		+	== Structural highlights ==
-	==~~Function~~==	+	<table><tr><td colspan='2'>[[4m55]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M55 FirstGlance]. <br>
-	[[~~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.~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
-		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lk3\|4lk3]]</td></tr>
-	==~~About this Structure~~==	+	<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>
-	[[4m55]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M55 OCA].	+	<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=4m55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m55 RCSB], [http://www.ebi.ac.uk/pdbsum/4m55 PDBsum]</span></td></tr>
		+	</table>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: UDP-glucuronate decarboxylase]]		[[Category: UDP-glucuronate decarboxylase]]
Line 15:		Line 19:
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Membrane]]		[[Category: Membrane]]
-	[[Category: ~~Rossman~~ fold]]	+	[[Category: Rossmann fold]]
	[[Category: Short-chain dehydrogenase/reductase]]		[[Category: Short-chain dehydrogenase/reductase]]

OCA at 07:41, 28 August 2013

OCA — Wed, 28 Aug 2013 07:41:07 GMT

←Older revision		Revision as of 07:41, 28 August 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4m55\| PDB=4m55 \| SCENE= }}
		+	===Crystal structure of Human UDP-xylose synthase R236H substitution===

-	~~The entry 4m55 is ON HOLD~~	+	==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.

-	~~Authors~~: ~~Walsh Jr~~.~~, R~~.M., Polizzi, S.J., Wood, Z.A.	+	==About this Structure==
-		+	[[4m55]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M55 OCA].
-	~~Description~~: ~~Crystal structure of Human UDP~~-~~xylose synthase R236H substitution~~	+	[[Category: Homo sapiens]]
		+	[[Category: UDP-glucuronate decarboxylase]]
		+	[[Category: Polizzi, S J.]]
		+	[[Category: Walsh, R M.]]
		+	[[Category: Wood, Z A.]]
		+	[[Category: Decarboxylase]]
		+	[[Category: Lyase]]
		+	[[Category: Membrane]]
		+	[[Category: Rossman fold]]
		+	[[Category: Short-chain dehydrogenase/reductase]]

OCA: Protected "4m55" [edit=sysop:move=sysop]

OCA — Wed, 14 Aug 2013 07:27:01 GMT

Protected "4m55" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:27, 14 August 2013

OCA: New page: '''Unreleased structure''' The entry 4m55 is ON HOLD Authors: Walsh Jr., R.M., Polizzi, S.J., Wood, Z.A. Description: Crystal structure of Human UDP-xylose synthase R236H substitution

OCA — Wed, 14 Aug 2013 07:26:57 GMT

New page: '''Unreleased structure''' The entry 4m55 is ON HOLD Authors: Walsh Jr., R.M., Polizzi, S.J., Wood, Z.A. Description: Crystal structure of Human UDP-xylose synthase R236H substitution

New page

'''Unreleased structure'''

The entry 4m55 is ON HOLD

Authors: Walsh Jr., R.M., Polizzi, S.J., Wood, Z.A.

Description: Crystal structure of Human UDP-xylose synthase R236H substitution