5tke - Revision history

OCA at 13:04, 4 October 2023

OCA — Wed, 04 Oct 2023 13:04:24 GMT

←Older revision		Revision as of 13:04, 4 October 2023
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	<StructureSection load='5tke' size='340' side='right'caption='[[5tke]], [[Resolution\|resolution]] 2.48Å' scene=''>		<StructureSection load='5tke' size='340' side='right'caption='[[5tke]], [[Resolution\|resolution]] 2.48Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tke]] is a 2 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=5TKE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5TKE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tke]] is a 2 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=5TKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TKE FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~MGEA5~~, ~~HEXC, KIAA0679, MEA5 (~~[~~http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</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]] 2.481Å</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=5tke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tke OCA], [~~http~~://pdbe.org/5tke PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5tke RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5tke PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5tke 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=5tke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tke OCA], [https://pdbe.org/5tke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tke RCSB], [https://www.ebi.ac.uk/pdbsum/5tke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tke ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/OGA_HUMAN OGA_HUMAN]] Isoform 1: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:11148210). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714).<ref>PMID:11148210</ref> <ref>PMID:11788610</ref> <ref>PMID:20673219</ref> <ref>PMID:22365600</ref> <ref>PMID:24088714</ref> Isoform 3: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1.<ref>PMID:20673219</ref>	+	[https://www.uniprot.org/uniprot/OGA_HUMAN OGA_HUMAN] Isoform 1: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:11148210). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714).<ref>PMID:11148210</ref> <ref>PMID:11788610</ref> <ref>PMID:20673219</ref> <ref>PMID:22365600</ref> <ref>PMID:24088714</ref> Isoform 3: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1.<ref>PMID:20673219</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Jiang, J]]	+	[[Category: Jiang J]]
-	[[Category: Li, B]]	+	[[Category: Li B]]
-	~~[[Category: Hydrolase~~]]	+

OCA at 12:12, 23 September 2020

OCA — Wed, 23 Sep 2020 12:12:35 GMT

←Older revision		Revision as of 12:12, 23 September 2020
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	==Crystal Structure of Eukaryotic Hydrolase==		==Crystal Structure of Eukaryotic Hydrolase==
-	<StructureSection load='5tke' size='340' side='right' caption='[[5tke]], [[Resolution\|resolution]] 2.48Å' scene=''>	+	<StructureSection load='5tke' size='340' side='right'caption='[[5tke]], [[Resolution\|resolution]] 2.48Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tke]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TKE OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5TKE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tke]] is a 2 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=5TKE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TKE FirstGlance]. <br>
-	</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=5tke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tke OCA], [http://pdbe.org/5tke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tke RCSB], [http://www.ebi.ac.uk/pdbsum/5tke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tke ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MGEA5, HEXC, KIAA0679, MEA5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5tke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tke OCA], [http://pdbe.org/5tke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tke RCSB], [http://www.ebi.ac.uk/pdbsum/5tke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tke ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Jiang, J]]		[[Category: Jiang, J]]
	[[Category: Li, B]]		[[Category: Li, B]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 06:43, 5 April 2017

OCA — Wed, 05 Apr 2017 06:43:18 GMT

←Older revision		Revision as of 06:43, 5 April 2017
Line 8:		Line 8:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/OGA_HUMAN OGA_HUMAN]] Isoform 1: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:11148210). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714).<ref>PMID:11148210</ref> <ref>PMID:11788610</ref> <ref>PMID:20673219</ref> <ref>PMID:22365600</ref> <ref>PMID:24088714</ref> Isoform 3: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1.<ref>PMID:20673219</ref>		[[http://www.uniprot.org/uniprot/OGA_HUMAN OGA_HUMAN]] Isoform 1: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:11148210). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714).<ref>PMID:11148210</ref> <ref>PMID:11788610</ref> <ref>PMID:20673219</ref> <ref>PMID:22365600</ref> <ref>PMID:24088714</ref> Isoform 3: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1.<ref>PMID:20673219</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human O-GlcNAcase (hOGA) is the unique enzyme responsible for the hydrolysis of the O-linked beta-N-acetyl glucosamine (O-GlcNAc) modification, an essential protein glycosylation event that modulates the function of numerous cellular proteins in response to nutrients and stress. Here we report crystal structures of a truncated hOGA, which comprises the catalytic and stalk domains, in apo form, in complex with an inhibitor, and in complex with a glycopeptide substrate. We found that hOGA forms an unusual arm-in-arm homodimer in which the catalytic domain of one monomer is covered by the stalk domain of the sister monomer to create a substrate-binding cleft. Notably, the residues on the cleft surface afford extensive interactions with the peptide substrate in a recognition mode that is distinct from that of its bacterial homologs. These structures represent the first model of eukaryotic enzymes in the glycoside hydrolase 84 (GH84) family and provide a crucial starting point for understanding the substrate specificity of hOGA, which regulates a broad range of biological and pathological processes.
		+
		+	Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode.,Li B, Li H, Lu L, Jiang J Nat Struct Mol Biol. 2017 Mar 20. doi: 10.1038/nsmb.3390. PMID:28319083<ref>PMID:28319083</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5tke" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:46, 15 March 2017

OCA — Wed, 15 Mar 2017 21:46:48 GMT

←Older revision		Revision as of 21:46, 15 March 2017
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-	'''Unreleased structure'''

-	~~The entry~~ 5tke is ~~ON HOLD until Paper Publication~~	+	==Crystal Structure of Eukaryotic Hydrolase==
-		+	<StructureSection load='5tke' size='340' side='right' caption='[[5tke]], [[Resolution\|resolution]] 2.48Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5tke]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TKE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TKE FirstGlance]. <br>
-	~~Description~~:	+	</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=5tke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tke OCA], [http://pdbe.org/5tke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tke RCSB], [http://www.ebi.ac.uk/pdbsum/5tke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tke ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/OGA_HUMAN OGA_HUMAN]] Isoform 1: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:11148210). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714).<ref>PMID:11148210</ref> <ref>PMID:11788610</ref> <ref>PMID:20673219</ref> <ref>PMID:22365600</ref> <ref>PMID:24088714</ref> Isoform 3: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1.<ref>PMID:20673219</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Jiang, J]]
		+	[[Category: Li, B]]
		+	[[Category: Hydrolase]]

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

OCA — Wed, 19 Oct 2016 15:57:44 GMT

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

←Older revision

Revision as of 15:57, 19 October 2016

OCA: New page: '''Unreleased structure''' The entry 5tke is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

OCA — Wed, 19 Oct 2016 15:57:43 GMT

New page: '''Unreleased structure''' The entry 5tke is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5tke is ON HOLD until Paper Publication

Authors:

Description:
[[Category: Unreleased Structures]]