Journal
FEBS LETTERS
Volume 566, Issue 1-3, Pages 11-16Publisher
WILEY
DOI: 10.1016/j.febslet.2004.04.005
Keywords
cellulose degradation; glycoside hydrolase; carbohydrate-binding module; family 37 CBM
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We recently showed that some of the enzymes underpinning cellulose solubilization by Rundnacoccus albus 8 lack the conventional type of dockerin module characteristic of cellulosomal proteins and instead, bear an X domain of unknown function at their C-termini. We have now subcloned and expressed six X domains and showed that five of them bind to xylan, chitin, microcrystalline and phosphoric-acid swollen cellulose, as well as more heterogenous substrates such as alfalfa cell walls, banana stem and wheat straw. The X domain that did not bind to these substrates was derived from a family-5 glycoside hydrolase (Cel5G), which possesses two X domains in tandem. Whereas the internal X domain failed to bind to the substrates, the recombinant dyad exhibited markedly enhanced binding relative to that observed for the C-terminal X domain alone. The evidence supports a distinctive carbohydrate-binding role of broad specificity for this type of domain, and we propose a novel family (designated family 37) of carbohydrate-binding modules that appear to be peculiar to R. albus. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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