2vsn
From Proteopedia
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| - | [[Image:2vsn.png|left|200px]] | ||
| - | + | ==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=''> | ||
| + | == 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> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | < | + | </StructureSection> |
| - | [[Category: Xanthomonas campestris pv. campestris]] | + | [[Category: Large Structures]] |
| - | [[Category: Davies | + | [[Category: Xanthomonas campestris pv. campestris str. 8004]] |
| - | [[Category: He | + | [[Category: Davies GJ]] |
| - | [[Category: Macauley | + | [[Category: He Y]] |
| - | [[Category: Martinez-Fleites | + | [[Category: Macauley MS]] |
| - | [[Category: Shen | + | [[Category: Martinez-Fleites C]] |
| - | [[Category: Vocadlo | + | [[Category: Shen D]] |
| - | + | [[Category: Vocadlo D]] | |
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Current revision
Structure and topological arrangement of an O-GlcNAc transferase homolog: insight into molecular control of intracellular glycosylation
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