6rhe

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:17, 17 October 2024) (edit) (undo)
 
Line 8: Line 8:
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6rhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rhe OCA], [https://pdbe.org/6rhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rhe RCSB], [https://www.ebi.ac.uk/pdbsum/6rhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rhe ProSAT]</span></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=6rhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rhe OCA], [https://pdbe.org/6rhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rhe RCSB], [https://www.ebi.ac.uk/pdbsum/6rhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rhe ProSAT]</span></td></tr>
</table>
</table>
-
== Function ==
+
<div style="background-color:#fffaf0;">
-
[https://www.uniprot.org/uniprot/OGA_CLOP1 OGA_CLOP1] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.
+
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6rhe" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[O-GlcNAcase|O-GlcNAcase]]
*[[O-GlcNAcase|O-GlcNAcase]]
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

CpOGA D298N in complex with hOGA-derived S-GlcNAc peptide

PDB ID 6rhe

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools