2ydq
From Proteopedia
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- | [[ | + | ==CpOGA D298N in complex with hOGA-derived O-GlcNAc peptide== |
+ | <StructureSection load='2ydq' size='340' side='right' caption='[[2ydq]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
+ | == 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> | ||
+ | </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><br> | ||
+ | <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><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes. O-GlcNAc addition and removal is catalyzed by O-GlcNAc transferase and O-GlcNAcase, respectively. We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome. Strikingly, the peptides bind a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation. In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains. These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome. In addition, this work will aid development of O-GlcNAcase inhibitors that target the peptide binding site. | ||
- | + | 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> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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[[Category: Beta-N-acetylhexosaminidase]] | [[Category: Beta-N-acetylhexosaminidase]] | ||
[[Category: Clostridium perfringens]] | [[Category: Clostridium perfringens]] |
Revision as of 07:41, 14 May 2014
CpOGA D298N in complex with hOGA-derived O-GlcNAc peptide
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