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2cho
From Proteopedia
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| - | [[Image:2cho.png|left|200px]] | ||
| - | < | + | ==Bacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activity== |
| - | + | <StructureSection load='2cho' size='340' side='right'caption='[[2cho]], [[Resolution|resolution]] 1.85Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2cho]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CHO 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]] 1.85Å</td></tr> | |
| - | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2cho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cho OCA], [https://pdbe.org/2cho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cho RCSB], [https://www.ebi.ac.uk/pdbsum/2cho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cho ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/OGA_BACTN OGA_BACTN] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. | ||
| + | == 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/ch/2cho_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=2cho ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | O-GlcNAc is an abundant post-translational modification of serine and threonine residues of nucleocytoplasmic proteins. This modification, found only within higher eukaryotes, is a dynamic modification that is often reciprocal to phosphorylation. In a manner analogous to phosphatases, a glycoside hydrolase termed O-GlcNAcase cleaves O-GlcNAc from modified proteins. Enzymes with high sequence similarity to human O-GlcNAcase are also found in human pathogens and symbionts. We report the three-dimensional structure of O-GlcNAcase from the human gut symbiont Bacteroides thetaiotaomicron both in its native form and in complex with a mimic of the reaction intermediate. Mutagenesis and kinetics studies show that the bacterial enzyme, very similarly to its human counterpart, operates via an unusual 'substrate-assisted' catalytic mechanism, which will inform the rational design of enzyme inhibitors. | ||
| - | + | Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity.,Dennis RJ, Taylor EJ, Macauley MS, Stubbs KA, Turkenburg JP, Hart SJ, Black GN, Vocadlo DJ, Davies GJ Nat Struct Mol Biol. 2006 Apr;13(4):365-71. Epub 2006 Mar 26. PMID:16565725<ref>PMID:16565725</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2cho" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Bacteroides thetaiotaomicron VPI-5482]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Black GN]] | |
| - | == | + | [[Category: Davies GJ]] |
| - | + | [[Category: Dennis RJ]] | |
| - | + | [[Category: Hart SJ]] | |
| - | + | [[Category: Macauley MS]] | |
| - | < | + | [[Category: Stubbs KA]] |
| - | [[Category: Bacteroides thetaiotaomicron]] | + | [[Category: Taylor EJ]] |
| - | [[Category: | + | [[Category: Turkenburg JP]] |
| - | [[Category: Black | + | [[Category: Vocadlo DJ]] |
| - | [[Category: Davies | + | |
| - | [[Category: Dennis | + | |
| - | [[Category: Hart | + | |
| - | [[Category: Macauley | + | |
| - | [[Category: Stubbs | + | |
| - | [[Category: Taylor | + | |
| - | [[Category: Turkenburg | + | |
| - | [[Category: Vocadlo | + | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Bacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activity
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