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| | ==The crystal structure of the d307a mutant of glycoside Hydrolase (family 31) from ruminococcus obeum atcc 29174== | | ==The crystal structure of the d307a mutant of glycoside Hydrolase (family 31) from ruminococcus obeum atcc 29174== |
| - | <StructureSection load='3m6d' size='340' side='right' caption='[[3m6d]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='3m6d' size='340' side='right'caption='[[3m6d]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3m6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Blautia_obeum_atcc_29174 Blautia obeum atcc 29174]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M6D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3m6d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Blautia_obeum_ATCC_29174 Blautia obeum ATCC 29174]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M6D FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ffj|3ffj]], [[3m46|3m46]]</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]] 2.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RUMOBE_03919 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=411459 Blautia obeum ATCC 29174])</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=3m6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6d OCA], [https://pdbe.org/3m6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m6d RCSB], [https://www.ebi.ac.uk/pdbsum/3m6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m6d ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3m6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6d OCA], [http://pdbe.org/3m6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m6d RCSB], [http://www.ebi.ac.uk/pdbsum/3m6d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m6d ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A5ZY13_9FIRM A5ZY13_9FIRM] |
| | == 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: Blautia obeum atcc 29174]] | + | [[Category: Blautia obeum ATCC 29174]] |
| - | [[Category: Babnigg, G]] | + | [[Category: Large Structures]] |
| - | [[Category: Freeman, L]] | + | [[Category: Babnigg G]] |
| - | [[Category: Joachimiak, A]] | + | [[Category: Freeman L]] |
| - | [[Category: Structural genomic]] | + | [[Category: Joachimiak A]] |
| - | [[Category: Tan, K]] | + | [[Category: Tan K]] |
| - | [[Category: Tesar, C]] | + | [[Category: Tesar C]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mcsg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| Structural highlights
Function
A5ZY13_9FIRM
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
The human intestine harbors a large number of microbes forming a complex microbial community that greatly affects the physiology and pathology of the host. In the human gut microbiome, the enrichment in certain protein gene families appears to be widespread. They include enzymes involved in carbohydrate metabolism such as glucoside hydrolases of dietary polysaccharides and glycoconjugates. We report the crystal structures (wild type, 2 mutants, and a mutant/substrate complex) and the enzymatic activity of a recombinant alpha-glucosidase from human gut bacterium Ruminococcus obeum. The first ever protein structures from this bacterium reveal a structural homologue to human intestinal maltase-glucoamylase with a highly conserved catalytic domain and reduced auxiliary domains. The alpha-glucosidase, a member of GH31 family, shows substrate preference for alpha(1-6) over alpha(1-4) glycosidic linkages and produces glucose from isomaltose as well as maltose. The preference can be switched by a single mutation at its active site, suggestive of widespread adaptation to utilization of a variety of polysaccharides by intestinal micro-organisms as energy resources.
Novel alpha-glucosidase from human gut microbiome: substrate specificities and their switch.,Tan K, Tesar C, Wilton R, Keigher L, Babnigg G, Joachimiak A FASEB J. 2010 Oct;24(10):3939-49. Epub 2010 Jun 25. PMID:20581222[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tan K, Tesar C, Wilton R, Keigher L, Babnigg G, Joachimiak A. Novel alpha-glucosidase from human gut microbiome: substrate specificities and their switch. FASEB J. 2010 Oct;24(10):3939-49. Epub 2010 Jun 25. PMID:20581222 doi:10.1096/fj.10-156257
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