2xsa: Difference between revisions
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< | ==OgOGA apostructure== | ||
<StructureSection load='2xsa' size='340' side='right'caption='[[2xsa]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xsa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oceanicola_granulosus_HTCC2516 Oceanicola granulosus HTCC2516]. The September 2011 RCSB PDB [https://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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2XSA FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=2xsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsa OCA], [https://pdbe.org/2xsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xsa RCSB], [https://www.ebi.ac.uk/pdbsum/2xsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xsa ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/OGA_OCEGH OGA_OCEGH] Cleaves GlcNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrate (in vitro).<ref>PMID:20863279</ref> | |||
<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> | |||
<div class="pdbe-citations 2xsa" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[O-GlcNAcase|O-GlcNAcase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[ | [[Category: O-GlcNAc Transferase]] | ||
[[Category: Oceanicola granulosus HTCC2516]] | |||
== | [[Category: RCSB PDB Molecule of the Month]] | ||
< | [[Category: Schuttelkopf AW]] | ||
[[Category: | [[Category: Van Aalten DMF]] | ||
[[Category: Oceanicola granulosus]] | |||
[[Category: | |||
[[Category: Schuttelkopf | |||
Latest revision as of 16:59, 1 February 2024
OgOGA apostructureOgOGA apostructure
Structural highlights
FunctionOGA_OCEGH Cleaves GlcNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrate (in vitro).[1] 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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