2xsa

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[[Image:2xsa.png|left|200px]]
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==OGOGA APOSTRUCTURE==
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<StructureSection load='2xsa' size='340' side='right' caption='[[2xsa]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2xsa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oceanicola_granulosus Oceanicola granulosus]. The September 2011 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''O-GlcNAc Transferase'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2011_9 10.2210/rcsb_pdb/mom_2011_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XSA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xsb|2xsb]]</td></tr>
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<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>
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<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=2xsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xsa RCSB], [http://www.ebi.ac.uk/pdbsum/2xsa PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes. O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or beta-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms. In the present study, we uncovered the first insights into the mechanism of substrate recognition by human OGA. The structure of a novel bacterial OGA orthologue reveals a putative substrate-binding groove, conserved in metazoan OGAs. Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-beta-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay. The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
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{{STRUCTURE_2xsa| PDB=2xsa | SCENE= }}
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Human OGA binds substrates in a conserved peptide recognition groove.,Schimpl M, Schuttelkopf AW, Borodkin VS, van Aalten DM Biochem J. 2010 Oct 25;432(1):1-7. PMID:20863279<ref>PMID:20863279</ref>
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===OGOGA APOSTRUCTURE===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_20863279}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2xsa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oceanicola_granulosus Oceanicola granulosus]. The September 2011 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''O-GlcNAc Transferase'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2011_9 10.2210/rcsb_pdb/mom_2011_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSA OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:020863279</ref><references group="xtra"/>
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[[Category: Beta-N-acetylhexosaminidase]]
[[Category: Beta-N-acetylhexosaminidase]]
[[Category: O-GlcNAc Transferase]]
[[Category: O-GlcNAc Transferase]]
[[Category: Oceanicola granulosus]]
[[Category: Oceanicola granulosus]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Aalten, D M.F Van.]]
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[[Category: Aalten, D M.F Van]]
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[[Category: Schuttelkopf, A W.]]
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[[Category: Schuttelkopf, A W]]
[[Category: Glycosyl hydrolase]]
[[Category: Glycosyl hydrolase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: O-glcnacase]]
[[Category: O-glcnacase]]
[[Category: O-glcnacylation]]
[[Category: O-glcnacylation]]

Revision as of 10:58, 25 January 2015

OGOGA APOSTRUCTURE

2xsa, resolution 2.00Å

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