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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=6f8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f8z OCA], [http://pdbe.org/6f8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f8z RCSB], [http://www.ebi.ac.uk/pdbsum/6f8z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f8z 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=6f8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f8z OCA], [http://pdbe.org/6f8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f8z RCSB], [http://www.ebi.ac.uk/pdbsum/6f8z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f8z ProSAT]</span></td></tr> | ||
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<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A dominant human gut microbe, the well studied symbiont Bacteroides thetaiotaomicron (Bt), is a glyco-specialist that harbors a large repertoire of genes devoted to carbohydrate processing. Despite strong similarities among them, many of the encoded enzymes have evolved distinct substrate specificities, and through the clustering of cognate genes within operons termed polysaccharide-utilization loci (PULs) enable the fulfilment of complex biological roles. Structural analyses of two glycoside hydrolase family 92 alpha-mannosidases, BT3130 and BT3965, together with mechanistically relevant complexes at 1.8-2.5 A resolution reveal conservation of the global enzyme fold and core catalytic apparatus despite different linkage specificities. Structure comparison shows that Bt differentiates the activity of these enzymes through evolution of a highly variable substrate-binding region immediately adjacent to the active site. These observations unveil a genetic/biochemical mechanism through which polysaccharide-processing bacteria can evolve new and specific biochemical activities from otherwise highly similar gene products. | |||
Bacteroides thetaiotaomicron generates diverse alpha-mannosidase activities through subtle evolution of a distal substrate-binding motif.,Thompson AJ, Spears RJ, Zhu Y, Suits MDL, Williams SJ, Gilbert HJ, Davies GJ Acta Crystallogr D Struct Biol. 2018 May 1;74(Pt 5):394-404. doi:, 10.1107/S2059798318002942. Epub 2018 Apr 24. PMID:29717710<ref>PMID:29717710</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 6f8z" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 09:35, 9 May 2018
Structure of the family GH92 alpha-mannosidase BT3130 from Bacteroides thetaiotaomicronStructure of the family GH92 alpha-mannosidase BT3130 from Bacteroides thetaiotaomicron
Structural highlights
Publication Abstract from PubMedA dominant human gut microbe, the well studied symbiont Bacteroides thetaiotaomicron (Bt), is a glyco-specialist that harbors a large repertoire of genes devoted to carbohydrate processing. Despite strong similarities among them, many of the encoded enzymes have evolved distinct substrate specificities, and through the clustering of cognate genes within operons termed polysaccharide-utilization loci (PULs) enable the fulfilment of complex biological roles. Structural analyses of two glycoside hydrolase family 92 alpha-mannosidases, BT3130 and BT3965, together with mechanistically relevant complexes at 1.8-2.5 A resolution reveal conservation of the global enzyme fold and core catalytic apparatus despite different linkage specificities. Structure comparison shows that Bt differentiates the activity of these enzymes through evolution of a highly variable substrate-binding region immediately adjacent to the active site. These observations unveil a genetic/biochemical mechanism through which polysaccharide-processing bacteria can evolve new and specific biochemical activities from otherwise highly similar gene products. Bacteroides thetaiotaomicron generates diverse alpha-mannosidase activities through subtle evolution of a distal substrate-binding motif.,Thompson AJ, Spears RJ, Zhu Y, Suits MDL, Williams SJ, Gilbert HJ, Davies GJ Acta Crystallogr D Struct Biol. 2018 May 1;74(Pt 5):394-404. doi:, 10.1107/S2059798318002942. Epub 2018 Apr 24. PMID:29717710[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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