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| | ==Sialidase BT_1020== | | ==Sialidase BT_1020== |
| - | <StructureSection load='5mqs' size='340' side='right' caption='[[5mqs]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='5mqs' size='340' side='right'caption='[[5mqs]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mqs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_thetaiotaomicron"_distaso_1912 "bacillus thetaiotaomicron" distaso 1912]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MQS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MQS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mqs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron Bacteroides thetaiotaomicron]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MQS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AHR:ALPHA-L-ARABINOFURANOSE'>AHR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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]] 3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AHR:ALPHA-L-ARABINOFURANOSE'>AHR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hypBA2, Btheta7330_02635 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=818 "Bacillus thetaiotaomicron" Distaso 1912])</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=5mqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mqs OCA], [https://pdbe.org/5mqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mqs RCSB], [https://www.ebi.ac.uk/pdbsum/5mqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mqs ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(Ara-f)(3)-Hyp_beta-L-arabinobiosidase (Ara-f)(3)-Hyp beta-L-arabinobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.187 3.2.1.187] </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=5mqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mqs OCA], [http://pdbe.org/5mqs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mqs RCSB], [http://www.ebi.ac.uk/pdbsum/5mqs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mqs ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8A8Z7_BACTN Q8A8Z7_BACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus thetaiotaomicron distaso 1912]] | + | [[Category: Bacteroides thetaiotaomicron]] |
| - | [[Category: Basle, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Cartmell, A]] | + | [[Category: Basle A]] |
| - | [[Category: Gilbert, H J]] | + | [[Category: Cartmell A]] |
| - | [[Category: Labourel, A]] | + | [[Category: Gilbert HJ]] |
| - | [[Category: Luis, A S]] | + | [[Category: Labourel A]] |
| - | [[Category: Ndeh, D]] | + | [[Category: Luis AS]] |
| - | [[Category: Rogowski, A]] | + | [[Category: Ndeh D]] |
| - | [[Category: Venditto, I]] | + | [[Category: Rogowski A]] |
| - | [[Category: Arabinofuranosidase]]
| + | [[Category: Venditto I]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Plant pectin]]
| + | |
| - | [[Category: Sialidase]]
| + | |
| Structural highlights
Function
Q8A8Z7_BACTN
Publication Abstract from PubMed
The metabolism of carbohydrate polymers drives microbial diversity in the human gut microbiota. It is unclear, however, whether bacterial consortia or single organisms are required to depolymerize highly complex glycans. Here we show that the gut bacterium Bacteroides thetaiotaomicron uses the most structurally complex glycan known: the plant pectic polysaccharide rhamnogalacturonan-II, cleaving all but 1 of its 21 distinct glycosidic linkages. The deconstruction of rhamnogalacturonan-II side chains and backbone are coordinated to overcome steric constraints, and the degradation involves previously undiscovered enzyme families and catalytic activities. The degradation system informs revision of the current structural model of rhamnogalacturonan-II and highlights how individual gut bacteria orchestrate manifold enzymes to metabolize the most challenging glycan in the human diet.
Complex pectin metabolism by gut bacteria reveals novel catalytic functions.,Ndeh D, Rogowski A, Cartmell A, Luis AS, Basle A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neill MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, Gilbert HJ Nature. 2017 Mar 22. doi: 10.1038/nature21725. PMID:28329766[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ndeh D, Rogowski A, Cartmell A, Luis AS, Basle A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neill MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, Gilbert HJ. Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature. 2017 Mar 22. doi: 10.1038/nature21725. PMID:28329766 doi:http://dx.doi.org/10.1038/nature21725
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