Ab initio structure determination and functional characterization of CBM36: A new family of calcium-dependent carbohydrate binding modules

S Jamal-Talabani, A B Boraston, J P Turkenburg, N Tarbouriech, V M A Ducros, G J Davies

Research output: Contribution to journalArticlepeer-review

Abstract

The enzymatic degradation of polysaccharides harnesses multimodular enzymes whose carbohydrate binding modules (CBM) target the catalytic domain onto the recalcitrant substrate. Here we report the ab initio structure determination and subsequent refinement, at 0.8 Angstrom resolution, of the CBM36 domain of the Paenibacillus polymyxa xylanase 43A. Affinity electrophoresis, isothermal titration calorimetry, and UV difference spectroscopy demonstrate that CBM36 is a novel Call-dependent xylan binding domain. The 3D structure of CBM36 in complex with xylotriose and Ca2+, at 1.5 Angstrom resolution, displays significant conformational changes compared to the native structure and reveals the molecular basis for its unique Ca2+-dependent binding of xylooligosaccharides through coordination of the O2 and O3 hydroxyls. CBM36 is one of an emerging spectrum of carbohydrate binding modules that increasingly find applications in industry and display great potential for mapping the "glyco-architecture" of plant cells.

Original languageEnglish
Pages (from-to)1177-1187
Number of pages11
JournalStructure
Volume12
Issue number7
Publication statusPublished - Jul 2004

Keywords

  • PROTEIN STRUCTURES
  • BACILLUS-POLYMYXA
  • LIGAND-BINDING
  • GLUCAN-BINDING
  • CELLULOSE
  • DOMAINS
  • HYDROLYSIS
  • REFINEMENT
  • SEQUENCE
  • COEFFICIENTS

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