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On the distinct binding modes of expansin and carbohydrate-binding module proteins on crystalline and nanofibrous cellulose: implications for cellulose degradation by designer cellulosomes.

Adam Orłowski,Lior Artzi,Pierre-André Cazade,Melissabye Gunnoo,E. Bayer,Damien Thompson

Published 2018 in Physical Chemistry, Chemical Physics - PCCP

ABSTRACT

Transformation of cellulose into monosaccharides can be achieved by hydrolysis of the cellulose chains, carried out by a special group of enzymes known as cellulases. The enzymatic mechanism of cellulases is well described, but the role of non-enzymatic components of the cellulose-degradation machinery is still poorly understood, and difficult to measure using experiments alone. In this study, we use a comprehensive set of atomistic molecular dynamics simulations to probe the molecular details of binding of the family-3a carbohydrate-binding module (CBM3a) and the bacterial expansin protein (EXLX1) to a range of cellulose substrates. Our results suggest that CBM3a behaves in a similar way on both crystalline and amorphous cellulose, whereas binding of the dual-domain expansin protein depends on the substrate crystallinity, and we relate our computed binding modes to the experimentally measured features of CBM and expansin action on cellulose.

PUBLICATION RECORD

  • Publication year

    2018

  • Venue

    Physical Chemistry, Chemical Physics - PCCP

  • Publication date

    2018-03-21

  • Fields of study

    Biology, Materials Science, Chemistry, Environmental Science, Medicine

  • Identifiers
    DOI 10.1039/c7cp07764ePMID 29528340
  • External record

    Open on Semantic Scholar

  • Source metadata

    Semantic Scholar, PubMed

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