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2ydq
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ydq' size='340' side='right' caption='[[2ydq]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2ydq' size='340' side='right' caption='[[2ydq]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ydq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YDQ OCA]. <br> | + | <table><tr><td colspan='2'>[[2ydq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YDQ FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cbi|2cbi]], [[2vur|2vur]], [[2x0y|2x0y]], [[2xpk|2xpk]], [[2j62|2j62]], [[2jh2|2jh2]], [[2wb5|2wb5]], [[2v5c|2v5c]], [[2cbj|2cbj]], [[2v5d|2v5d]], [[2yds|2yds]], [[2ydr|2ydr]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cbi|2cbi]], [[2vur|2vur]], [[2x0y|2x0y]], [[2xpk|2xpk]], [[2j62|2j62]], [[2jh2|2jh2]], [[2wb5|2wb5]], [[2v5c|2v5c]], [[2cbj|2cbj]], [[2v5d|2v5d]], [[2yds|2yds]], [[2ydr|2ydr]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ydq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ydq RCSB], [http://www.ebi.ac.uk/pdbsum/2ydq 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=2ydq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ydq RCSB], [http://www.ebi.ac.uk/pdbsum/2ydq PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/OGA_CLOP1 OGA_CLOP1]] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. [[http://www.uniprot.org/uniprot/NCOAT_HUMAN NCOAT_HUMAN]] Cleaves GlcNAc but not GalNAc from glycopeptides. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc. Possesses hyaluronidase activity. Acetylates 'Lys-8' of histone H4 and 'Lys-14' of histone H3.<ref>PMID:11148210</ref> <ref>PMID:11788610</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition.,Schimpl M, Borodkin VS, Gray LJ, van Aalten DM Chem Biol. 2012 Feb 24;19(2):173-8. PMID:22365600<ref>PMID:22365600</ref> | Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition.,Schimpl M, Borodkin VS, Gray LJ, van Aalten DM Chem Biol. 2012 Feb 24;19(2):173-8. PMID:22365600<ref>PMID:22365600</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
| Line 22: | Line 24: | ||
[[Category: Beta-N-acetylhexosaminidase]] | [[Category: Beta-N-acetylhexosaminidase]] | ||
[[Category: Clostridium perfringens]] | [[Category: Clostridium perfringens]] | ||
| - | [[Category: Aalten, D M.F Van | + | [[Category: Aalten, D M.F Van]] |
| - | [[Category: Borodkin, V S | + | [[Category: Borodkin, V S]] |
| - | [[Category: Gray, L J | + | [[Category: Gray, L J]] |
| - | [[Category: Schimpl, M | + | [[Category: Schimpl, M]] |
[[Category: Hydrolase-peptide complex]] | [[Category: Hydrolase-peptide complex]] | ||
Revision as of 19:16, 25 December 2014
CpOGA D298N in complex with hOGA-derived O-GlcNAc peptide
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