2xsb: Difference between revisions
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[[ | ==OGOGA PUGNAC COMPLEX== | ||
<StructureSection load='2xsb' size='340' side='right' caption='[[2xsb]], [[Resolution|resolution]] 2.11Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xsb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oceanicola_granulosus Oceanicola granulosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XSB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xsa|2xsa]]</td></tr> | |||
<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 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=2xsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xsb RCSB], [http://www.ebi.ac.uk/pdbsum/2xsb PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Beta-N-acetylhexosaminidase]] | [[Category: Beta-N-acetylhexosaminidase]] | ||
[[Category: Oceanicola granulosus]] | [[Category: Oceanicola granulosus]] | ||
[[Category: Aalten, D M.F Van | [[Category: Aalten, D M.F Van]] | ||
[[Category: Schuttelkopf, A W | [[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 11:04, 12 November 2014
OGOGA PUGNAC COMPLEXOGOGA PUGNAC COMPLEX
Structural highlights
Publication Abstract from PubMedModification 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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