2vsn: Difference between revisions
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< | ==Structure and topological arrangement of an O-GlcNAc transferase homolog: insight into molecular control of intracellular glycosylation== | ||
<StructureSection load='2vsn' size='340' side='right'caption='[[2vsn]], [[Resolution|resolution]] 2.75Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vsn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris_str._8004 Xanthomonas campestris pv. campestris str. 8004]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VSN 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]] 2.75Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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=2vsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vsn OCA], [https://pdbe.org/2vsn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vsn RCSB], [https://www.ebi.ac.uk/pdbsum/2vsn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vsn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H2XAK3_XANC8 A0A0H2XAK3_XANC8] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vs/2vsn_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vsn ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
N-Acetylglucosamine (O-GlcNAc) modification of proteins provides a mechanism for the control of diverse cellular processes through a dynamic interplay with phosphorylation. UDP-GlcNAc:polypeptidyl transferase (OGT) catalyzes O-GlcNAc addition. The structure of an intact OGT homolog and kinetic analysis of human OGT variants reveal a contiguous superhelical groove that directs substrates to the active site. | |||
Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation.,Martinez-Fleites C, Macauley MS, He Y, Shen DL, Vocadlo DJ, Davies GJ Nat Struct Mol Biol. 2008 Jul;15(7):764-5. Epub 2008 Jun 8. PMID:18536723<ref>PMID:18536723</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
<div class="pdbe-citations 2vsn" style="background-color:#fffaf0;"></div> | |||
[[Category: Xanthomonas campestris pv. campestris]] | == References == | ||
[[Category: Davies | <references/> | ||
[[Category: He | __TOC__ | ||
[[Category: Macauley | </StructureSection> | ||
[[Category: Martinez-Fleites | [[Category: Large Structures]] | ||
[[Category: Shen | [[Category: Xanthomonas campestris pv. campestris str. 8004]] | ||
[[Category: Vocadlo | [[Category: Davies GJ]] | ||
[[Category: He Y]] | |||
[[Category: Macauley MS]] | |||
[[Category: Martinez-Fleites C]] | |||
[[Category: Shen D]] | |||
[[Category: Vocadlo D]] | |||