Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/13561
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Type: Journal article
Title: Comparative modeling of the three-dimensional structures of family 3 glycoside hydrolases
Author: Harvey, A.
Hrmova, M.
De Gori, R.
Varghese, J.
Fincher, G.
Citation: Proteins-Structure Function and Genetics, 2000; 41(2):257-269
Publisher: Wiley-Liss
Issue Date: 2000
ISSN: 0887-3585
1097-0134
Abstract: There are approximately 100 known members of the family 3 group of glycoside hydrolases, most of which are classified as beta-glucosidases and originate from microorganisms. The only family 3 glycoside hydrolase for which a three-dimensional structure is available is a beta-glucan exohydrolase from barley. The structural coordinates of the barley enzyme is used here to model representatives from distinct phylogenetic clusters within the family. The majority of family 3 hydrolases have an NH(2)-terminal (alpha/beta)(8) barrel connected by a short linker to a second domain, which adopts an (alpha/beta)(6) sandwich fold. In two bacterial beta-glucosidases, the order of the domains is reversed. The catalytic nucleophile, equivalent to D285 of the barley beta-glucan exohydrolase, is absolutely conserved across the family. It is located on domain 1, in a shallow site pocket near the interface of the domains. The likely catalytic acid in the barley enzyme, E491, is on domain 2. Although similarly positioned acidic residues are present in closely related members of the family, the equivalent amino acid in more distantly related members is either too far from the active site or absent. In the latter cases, the role of catalytic acid is probably assumed by other acidic amino acids from domain 1.
Keywords: Glycoside Hydrolases; beta-Glucosidase; Cellulase; Cellulose 1,4-beta-Cellobiosidase; Sequence Alignment; Evolution, Molecular; Phylogeny; Amino Acid Sequence; Catalytic Domain; Conserved Sequence; Models, Molecular; Molecular Sequence Data
RMID: 0001000219
DOI: 10.1002/1097-0134(20001101)41:2<257::AID-PROT100>3.0.CO;2-C
Appears in Collections:Agriculture, Food and Wine publications

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