Structural basis for cellulose binding by the type A carbohydrate-binding module 64 of Spirochaeta thermophila

André Schiefner, Angel Angelov, Wolfgang Liebl, Arne Skerra

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

Spirochaeta thermophila secretes seven glycoside hydrolases for plant biomass degradation that carry a carbohydrate-binding module 64 (CBM64) appended at the C-terminus. CBM64 adsorbs to various β1-4-linked pyranose substrates and shows high affinity for cellulose. We present the first crystal structure of a CBM64 at 1.2 Å resolution, which reveals a jelly-roll-like fold corresponding to a surface-binding type A CBM. Modeling of its interaction with cellulose indicates that CBM64 achieves association with the hydrophobic face of β-linked pyranose chains via a unique coplanar arrangement of four exposed tryptophan side chains.

Original languageEnglish
Pages (from-to)855-858
Number of pages4
JournalProteins: Structure, Function and Bioinformatics
Volume84
Issue number6
DOIs
StatePublished - 1 Jun 2016

Keywords

  • CBM64
  • Carbohydrate-binding module
  • Cellulose-binding domain
  • Type A CBM
  • β-sandwich

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