2cho: Difference between revisions

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-[[Image:2cho.gif|left|200px]]<br />
-<applet load="2cho" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2cho, resolution 1.85&Aring;" />
-'''BACTEROIDES THETAIOTAOMICRON HEXOSAMINIDASE WITH O-GLCNACASE ACTIVITY'''<br />
-==Overview==
+==Bacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activity==
-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.
+<StructureSection load='2cho' size='340' side='right'caption='[[2cho]], [[Resolution|resolution]] 1.85&Aring;' 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]] 1.85&#8491;</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.
-==About this Structure==
+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>
-CHO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron Bacteroides thetaiotaomicron] with CA, ACT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CHO OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16565725 16565725]
+</div>
-[[Category: Bacteroides thetaiotaomicron]]
+<div class="pdbe-citations 2cho" style="background-color:#fffaf0;"></div>
-[[Category: Beta-N-acetylhexosaminidase]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: Black, G.N.]]
+__TOC__
-[[Category: Davies, G.J.]]
+</StructureSection>
-[[Category: Dennis, R.J.]]
+[[Category: Bacteroides thetaiotaomicron VPI-5482]]
-[[Category: Hart, S.J.]]
+[[Category: Large Structures]]
-[[Category: Macauley, M.S.]]
+[[Category: Black GN]]
-[[Category: Stubbs, K.A.]]
+[[Category: Davies GJ]]
-[[Category: Taylor, E.J.]]
+[[Category: Dennis RJ]]
-[[Category: Turkenburg, J.P.]]
+[[Category: Hart SJ]]
-[[Category: Vocadlo, D.J.]]
+[[Category: Macauley MS]]
-[[Category: ACT]]
+[[Category: Stubbs KA]]
-[[Category: CA]]
+[[Category: Taylor EJ]]
-[[Category: GOL]]
+[[Category: Turkenburg JP]]
-[[Category: hydrolase]]
+[[Category: Vocadlo DJ]]
-[[Category: n-acetylglucosamine]]
-[[Category: o-glcnacase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 18:09:22 2007''