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

Mercedes C Hernandez-Gomez, Maja G Rydahl, Artur Rogowski, Carl Morland, Alan Cartmell, Lucy Crouch, Aurore Labourel, Carlos M G A Fontes, William G T Willats, Harry J Gilbert, J Paul Knox

FEBS letters 2015 Aug 19

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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. Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Citation

Mercedes C Hernandez-Gomez, Maja G Rydahl, Artur Rogowski, Carl Morland, Alan Cartmell, Lucy Crouch, Aurore Labourel, Carlos M G A Fontes, William G T Willats, Harry J Gilbert, J Paul Knox. Recognition of xyloglucan by the crystalline cellulose-binding site of a family 3a carbohydrate-binding module. FEBS letters. 2015 Aug 19;589(18):2297-303