4zxl
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CpOGA D298N in complex with Drosophila HCF -derived Thr-O-GlcNAc peptide== | |
| + | <StructureSection load='4zxl' size='340' side='right' caption='[[4zxl]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4zxl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clop1 Clop1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZXL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZXL FirstGlance]. <br> | ||
| + | </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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yds|2yds]], [[2ydr|2ydr]], [[2ydq|2ydq]], [[2vur|2vur]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nagJ, CPF_1442 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=195103 CLOP1])</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=4zxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zxl OCA], [http://pdbe.org/4zxl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zxl RCSB], [http://www.ebi.ac.uk/pdbsum/4zxl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zxl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/OGA_CLOP1 OGA_CLOP1]] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | O-GlcNAcylation is a reversible type of serine/threonine glycosylation on nucleocytoplasmic proteins in metazoa. Various genetic approaches in several animal models have revealed that O-GlcNAcylation is essential for embryogenesis. However, the dynamic changes in global O-GlcNAcylation and the underlying mechanistic biology linking them to embryonic development is not understood. One of the limiting factors towards characterizing changes in O-GlcNAcylation has been the limited specificity of currently available tools to detect this modification. In the present study, harnessing the unusual properties of an O-GlcNAcase (OGA) mutant that binds O-GlcNAc (O-N-acetylglucosamine) sites with nanomolar affinity, we uncover changes in protein O-GlcNAcylation as a function of Drosophila development. | ||
| - | + | A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development.,Mariappa D, Selvan N, Borodkin V, Alonso J, Ferenbach AT, Shepherd C, Navratilova IH, vanAalten DMF Biochem J. 2015 Sep 1;470(2):255-262. doi: 10.1042/BJ20150610. Epub 2015 Jul 14. PMID:26348912<ref>PMID:26348912</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 4zxl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Clop1]] | ||
| + | [[Category: Aalten, D M.F van]] | ||
[[Category: Selvan, N]] | [[Category: Selvan, N]] | ||
| - | [[Category: | + | [[Category: Hydrolase-o-glcnacylated peptide complex tim barrel thr-o-glcnac]] |
| + | [[Category: Hydrolase-peptide complex]] | ||
Revision as of 15:32, 16 November 2017
CpOGA D298N in complex with Drosophila HCF -derived Thr-O-GlcNAc peptide
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