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| | <StructureSection load='2wvy' size='340' side='right'caption='[[2wvy]], [[Resolution|resolution]] 2.26Å' scene=''> | | <StructureSection load='2wvy' size='340' side='right'caption='[[2wvy]], [[Resolution|resolution]] 2.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wvy]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bactn Bactn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WVY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wvy]] is a 3 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=2WVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WVY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ww3|2ww3]], [[2ww2|2ww2]], [[2wvz|2wvz]], [[2wvx|2wvx]], [[2ww1|2ww1]], [[2ww0|2ww0]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wvy OCA], [http://pdbe.org/2wvy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wvy RCSB], [http://www.ebi.ac.uk/pdbsum/2wvy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wvy ProSAT]</span></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=2wvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wvy OCA], [https://pdbe.org/2wvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wvy RCSB], [https://www.ebi.ac.uk/pdbsum/2wvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wvy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8A5N9_BACTN Q8A5N9_BACTN] |
| | == 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: Bactn]] | + | [[Category: Bacteroides thetaiotaomicron VPI-5482]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Davies, G J]] | + | [[Category: Davies GJ]] |
| - | [[Category: Gilbert, H J]] | + | [[Category: Gilbert HJ]] |
| - | [[Category: Suits, M D.L]] | + | [[Category: Suits MDL]] |
| - | [[Category: Thompson, A]] | + | [[Category: Thompson A]] |
| - | [[Category: Zhu, Y]] | + | [[Category: Zhu Y]] |
| - | [[Category: Bt3990]]
| + | |
| - | [[Category: Gh92]]
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| - | [[Category: Glycoside hydrolase family 92]]
| + | |
| - | [[Category: Hydrolase]]
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| Structural highlights
Function
Q8A5N9_BACTN
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 PubMed
Colonic bacteria, exemplified by Bacteroides thetaiotaomicron, play a key role in maintaining human health by harnessing large families of glycoside hydrolases (GHs) to exploit dietary polysaccharides and host glycans as nutrients. Such GH family expansion is exemplified by the 23 family GH92 glycosidases encoded by the B. thetaiotaomicron genome. Here we show that these are alpha-mannosidases that act via a single displacement mechanism to utilize host N-glycans. The three-dimensional structure of two GH92 mannosidases defines a family of two-domain proteins in which the catalytic center is located at the domain interface, providing acid (glutamate) and base (aspartate) assistance to hydrolysis in a Ca(2+)-dependent manner. The three-dimensional structures of the GH92s in complex with inhibitors provide insight into the specificity, mechanism and conformational itinerary of catalysis. Ca(2+) plays a key catalytic role in helping distort the mannoside away from its ground-state (4)C(1) chair conformation toward the transition state.
Mechanistic insights into a Ca2+-dependent family of alpha-mannosidases in a human gut symbiont.,Zhu Y, Suits MD, Thompson AJ, Chavan S, Dinev Z, Dumon C, Smith N, Moremen KW, Xiang Y, Siriwardena A, Williams SJ, Gilbert HJ, Davies GJ Nat Chem Biol. 2010 Feb;6(2):125-32. Epub 2009 Dec 27. PMID:20081828[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhu Y, Suits MD, Thompson AJ, Chavan S, Dinev Z, Dumon C, Smith N, Moremen KW, Xiang Y, Siriwardena A, Williams SJ, Gilbert HJ, Davies GJ. Mechanistic insights into a Ca2+-dependent family of alpha-mannosidases in a human gut symbiont. Nat Chem Biol. 2010 Feb;6(2):125-32. Epub 2009 Dec 27. PMID:20081828 doi:10.1038/nchembio.278
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