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Bacteroides thetaiotaomicron generates diverse α-mannosidase activities through subtle evolution of a distal substrate-binding motif.
Thompson, Andrew J; Spears, Richard J; Zhu, Yanping; Suits, Michael D L; Williams, Spencer J; Gilbert, Harry J; Davies, Gideon J.
Affiliation
  • Thompson AJ; Department of Chemistry, University of York, Heslington, York YO10 5DD, England.
  • Spears RJ; Department of Chemistry, University of York, Heslington, York YO10 5DD, England.
  • Zhu Y; Institute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle-upon-Tyne NE2 4HH, England.
  • Suits MDL; Department of Chemistry, University of York, Heslington, York YO10 5DD, England.
  • Williams SJ; School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
  • Gilbert HJ; Institute for Cell and Molecular Biosciences, Newcastle University, Framlington Place, Newcastle-upon-Tyne NE2 4HH, England.
  • Davies GJ; Department of Chemistry, University of York, Heslington, York YO10 5DD, England.
Acta Crystallogr D Struct Biol ; 74(Pt 5): 394-404, 2018 May 01.
Article in En | MEDLINE | ID: mdl-29717710
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Genetic Variation / Evolution, Molecular / Alpha-Mannosidase / Bacteroides thetaiotaomicron Limits: Humans Language: En Journal: Acta Crystallogr D Struct Biol Year: 2018 Document type: Article
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Genetic Variation / Evolution, Molecular / Alpha-Mannosidase / Bacteroides thetaiotaomicron Limits: Humans Language: En Journal: Acta Crystallogr D Struct Biol Year: 2018 Document type: Article