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The Plant Cell, Vol. 14, 1033-1052, May 2002, Copyright © 2002,
American Society of Plant Biologists

Structural Basis for Broad Substrate Specificity in Higher Plant {beta}-D-Glucan Glucohydrolases

Maria Hrmovaa, Ross De Gorib, Brian J. Smithc, Jon K. Fairweatherd, Hugues Driguezd, Joseph N. Vargheseb and Geoffrey B. Fincher1,a

a Department of Plant Science, University of Adelaide, Waite Campus, Glen Osmond, South Australia 5064, Australia
b Commonwealth Scientific and Industrial Research Organization, Division of Health Sciences and Nutrition, 343 Royal Parade, Parkville, Victoria 3052, Australia
c The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3050, Australia
d Centre de Recherches sur les Macromolécules Végétales, Centre National de la Recherche Scientifique (affiliated with Université Joseph Fourier), BP 53, 38041 Grenoble cedex 09, France

1 To whom correspondence should be addressed. E-mail geoff.fincher{at}adelaide.edu.au; fax 61-8-8303-7109

Family 3 {beta}-D-glucan glucohydrolases are distributed widely in higher plants. The enzymes catalyze the hydrolytic removal of {beta}-D-glucosyl residues from nonreducing termini of a range of {beta}-D-glucans and {beta}-D-oligoglucosides. Their broad specificity can be explained by x-ray crystallographic data obtained from a barley {beta}-D-glucan glucohydrolase in complex with nonhydrolyzable S-glycoside substrate analogs and by molecular modeling of enzyme/substrate complexes. The glucosyl residue that occupies binding subsite -1 is locked tightly into a fixed position through extensive hydrogen bonding with six amino acid residues near the bottom of an active site pocket. In contrast, the glucosyl residue at subsite +1 is located between two Trp residues at the entrance of the pocket, where it is constrained less tightly. The relative flexibility of binding at subsite +1, coupled with the projection of the remainder of bound substrate away from the enzyme's surface, means that the overall active site can accommodate a range of substrates with variable spatial dispositions of adjacent {beta}-D-glucosyl residues. The broad specificity for glycosidic linkage type enables the enzyme to perform diverse functions during plant development.




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