Recognition of xyloglucan by the crystalline cellulose-binding site of a family 3a carbohydrate-binding module

FEBS Lett. 2015 Aug 19;589(18):2297-303. doi: 10.1016/j.febslet.2015.07.009. Epub 2015 Jul 18.

Abstract

Type A non-catalytic carbohydrate-binding modules (CBMs), exemplified by CtCBM3acipA, are widely believed to specifically target crystalline cellulose through entropic forces. Here we have tested the hypothesis that type A CBMs can also bind to xyloglucan (XG), a soluble β-1,4-glucan containing α-1,6-xylose side chains. CtCBM3acipA bound to xyloglucan in cell walls and arrayed on solid surfaces. Xyloglucan and cellulose were shown to bind to the same planar surface on CBM3acipA. A range of type A CBMs from different families were shown to bind to xyloglucan in solution with ligand binding driven by enthalpic changes. The nature of CBM-polysaccharide interactions is discussed.

Keywords: CBM3a; Carbohydrate-binding module; Crystalline cellulose; Plant cell wall; Xyloglucan.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Cell Wall / metabolism
  • Cellulose / chemistry*
  • Cellulose / metabolism*
  • Clostridium thermocellum
  • Glucans / chemistry
  • Glucans / metabolism*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Protein Binding
  • Solubility
  • Xylans / chemistry
  • Xylans / metabolism*

Substances

  • Bacterial Proteins
  • CipA protein, Clostridium
  • Glucans
  • Membrane Proteins
  • Xylans
  • xyloglucan
  • Cellulose