6rhe
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==CpOGA D298N in complex with hOGA-derived S-GlcNAc peptide== | |
| + | <StructureSection load='6rhe' size='340' side='right'caption='[[6rhe]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6rhe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RHE 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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_O-GlcNAcase Protein O-GlcNAcase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.169 3.2.1.169] </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=6rhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rhe OCA], [http://pdbe.org/6rhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rhe RCSB], [http://www.ebi.ac.uk/pdbsum/6rhe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rhe 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 == | ||
| + | Modification of specific Ser and Thr residues of nucleocytoplasmic proteins with O-GlcNAc, catalyzed by O-GlcNAc transferase (OGT), is an abundant posttranslational event essential for proper animal development and is dysregulated in various diseases. Due to the rapid concurrent removal by the single O-GlcNAcase (OGA), precise functional dissection of site-specific O-GlcNAc modification in vivo is currently not possible without affecting the entire O-GlcNAc proteome. Exploiting the fortuitous promiscuity of OGT, we show that S-GlcNAc is a hydrolytically stable and accurate structural mimic of O-GlcNAc that can be encoded in mammalian systems with CRISPR-Cas9 in an otherwise unperturbed O-GlcNAcome. Using this approach, we target an elusive Ser 405 O-GlcNAc site on OGA, showing that this site-specific modification affects OGA stability. | ||
| - | + | Genetic recoding to dissect the roles of site-specific protein O-GlcNAcylation.,Gorelik A, Bartual SG, Borodkin VS, Varghese J, Ferenbach AT, van Aalten DMF Nat Struct Mol Biol. 2019 Nov;26(11):1071-1077. doi: 10.1038/s41594-019-0325-8., Epub 2019 Nov 6. PMID:31695185<ref>PMID:31695185</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6rhe" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Protein O-GlcNAcase]] | ||
| + | [[Category: Aalten, D Van]] | ||
| + | [[Category: Bartual, S G]] | ||
| + | [[Category: Gorelik, A]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: N-acetyl glucosamine hidrolase]] | ||
Revision as of 09:15, 25 December 2019
CpOGA D298N in complex with hOGA-derived S-GlcNAc peptide
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