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 [https://en.wikipedia.org/wiki/Clostridium_perfringens_ATCC_13124 Clostridium perfringens ATCC 13124] and [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4ZXL 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]] 2.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4zxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zxl OCA], [https://pdbe.org/4zxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zxl RCSB], [https://www.ebi.ac.uk/pdbsum/4zxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zxl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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> |
| - | [[Category: Selvan | + | <div class="pdbe-citations 4zxl" style="background-color:#fffaf0;"></div> |
| - | [[Category: Van Aalten | + | |
| + | ==See Also== | ||
| + | *[[O-GlcNAcase|O-GlcNAcase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Clostridium perfringens ATCC 13124]] | ||
| + | [[Category: Drosophila melanogaster]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Selvan N]] | ||
| + | [[Category: Van Aalten DMF]] | ||
Current revision
CpOGA D298N in complex with Drosophila HCF -derived Thr-O-GlcNAc peptide
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