2ydr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:50, 20 December 2023) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2ydr.jpg|left|200px]]
 
-
<!--
+
==CpOGA D298N in complex with p53-derived O-GlcNAc peptide==
-
The line below this paragraph, containing "STRUCTURE_2ydr", creates the "Structure Box" on the page.
+
<StructureSection load='2ydr' size='340' side='right'caption='[[2ydr]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2ydr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YDR FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</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>
-
{{STRUCTURE_2ydr| PDB=2ydr | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ydr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydr OCA], [https://pdbe.org/2ydr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ydr RCSB], [https://www.ebi.ac.uk/pdbsum/2ydr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ydr 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 ==
 +
Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes. O-GlcNAc addition and removal is catalyzed by O-GlcNAc transferase and O-GlcNAcase, respectively. We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome. Strikingly, the peptides bind a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation. In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains. These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome. In addition, this work will aid development of O-GlcNAcase inhibitors that target the peptide binding site.
-
===CpOGA D298N in complex with p53-derived O-GlcNAc peptide===
+
Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition.,Schimpl M, Borodkin VS, Gray LJ, van Aalten DM Chem Biol. 2012 Feb 24;19(2):173-8. PMID:22365600<ref>PMID:22365600</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2ydr" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_22365600}}, adds the Publication Abstract to the page
+
*[[O-GlcNAcase|O-GlcNAcase]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 22365600 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_22365600}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
[[2ydr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YDR OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:022365600</ref><references group="xtra"/>
+
-
[[Category: Beta-N-acetylhexosaminidase]]
+
[[Category: Clostridium perfringens]]
[[Category: Clostridium perfringens]]
-
[[Category: Aalten, D M.F Van.]]
+
[[Category: Homo sapiens]]
-
[[Category: Borodkin, V S.]]
+
[[Category: Large Structures]]
-
[[Category: Gray, L J.]]
+
[[Category: Borodkin VS]]
-
[[Category: Schimpl, M.]]
+
[[Category: Gray LJ]]
-
[[Category: Cell cycle]]
+
[[Category: Schimpl M]]
-
[[Category: Hydrolase-peptide complex]]
+
[[Category: Van Aalten DMF]]

Current revision

CpOGA D298N in complex with p53-derived O-GlcNAc peptide

PDB ID 2ydr

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools