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Papers In Press, published online ahead of print October 22, 2004
Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6
Corresponding Author: boraston{at}uvic.ca
Enzymes that hydrolyse insoluble complex polysaccharide structures contain non-catalytic carbohydrate binding modules that play a pivotal role in the action of these enzymes against recalcitrant substrates. Family 6 CBMs (CBM6s), are distinct from other CBM families, in that these protein modules contain multiple distinct ligand binding sites, a feature that makes CBM6s particularly appropriate receptors for the
J. Biol. Chem, 10.1074/jbc.M410113200
Submitted on September 2, 2004
Revised on October 20, 2004
Accepted on October 22, 2004
Family 6 carbohydrate binding modules recognise the non-reducing end of
-1,3-linked glucans by presenting a unique ligand binding surface
-1,3-glucan laminarin, which displays an extended U-shaped conformation. To interrogate the mechanism by which family 6 CBMs recognise laminarin we report the biochemical and structural properties of a CBM6 (designated BhCBM6) that is located in an enzyme which is shown, in this work, to display -1,3-glucanase activity. BhCBM6 binds -1,3-glucooligosaccharides with affinities of ~1 x 105 M-1. The X-ray crystal structure of this CBM in complex with laminarihexaose, reveals similarity with the structures of other CBM6s but a unique binding mode. The binding cleft in this protein is sealed at one end, which prevents binding of linear polysaccharides such as cellulose and the orientation of the sugar at this site prevents glycone extension of the ligand and thus conferring specificity for the non-reducing ends of glycans. The high affinity for extended -1,3- glucooligosaccharides is conferred by interactions with the surface of the protein located between the two binding sites common to CBM6s and thus reveals a third ligand binding site in family 6 CBMs. This study therefore demonstrates how the multiple binding clefts and highly unusual protein surface of family 6 CBMs confers the extensive range of specificities displayed by this protein family. This is in sharp contrast to other families of CBMs where variation in specificity between different members reflects differences in the topology of a single binding site
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