5mt2
From Proteopedia
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<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=5mt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mt2 OCA], [http://pdbe.org/5mt2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mt2 RCSB], [http://www.ebi.ac.uk/pdbsum/5mt2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mt2 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=5mt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mt2 OCA], [http://pdbe.org/5mt2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mt2 RCSB], [http://www.ebi.ac.uk/pdbsum/5mt2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mt2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:28329766</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 5mt2" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 06:59, 5 April 2017
Glycoside hydrolase BT_0996
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