2cho: Difference between revisions
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==Bacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activity== | ==Bacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activity== | ||
<StructureSection load='2cho' size='340' side='right' caption='[[2cho]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='2cho' size='340' side='right'caption='[[2cho]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2cho]] is a 4 chain structure with sequence from [ | <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=' | </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=' | <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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacteroides thetaiotaomicron VPI-5482]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Black | [[Category: Black GN]] | ||
[[Category: Davies | [[Category: Davies GJ]] | ||
[[Category: Dennis | [[Category: Dennis RJ]] | ||
[[Category: Hart | [[Category: Hart SJ]] | ||
[[Category: Macauley | [[Category: Macauley MS]] | ||
[[Category: Stubbs | [[Category: Stubbs KA]] | ||
[[Category: Taylor | [[Category: Taylor EJ]] | ||
[[Category: Turkenburg | [[Category: Turkenburg JP]] | ||
[[Category: Vocadlo | [[Category: Vocadlo DJ]] | ||
Latest revision as of 12:25, 9 May 2024
Bacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activityBacteroides thetaiotaomicron hexosaminidase with O-GlcNAcase activity
Structural highlights
FunctionOGA_BACTN Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedO-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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