Three-dimensional modelling of the catalytic domain of Streptococcus mutans glucosyltransferase GtfB
Resource
FEMS Microbiology Letters 2000(188), 75-79
Journal
FEMS Microbiology Letters 2000(188)
Pages
75-79
Date Issued
2001
Date
2001
Author(s)
Lou, Kuo-Long
DOI
892314B002555
Abstract
Glucosyltransferases (GtfB/C/D) of Streptococcus mutans, a pathogen for human dental caries, synthesize water-insoluble glucan through
the hydrolysis of sucrose. Genetic and biochemical approaches have identified several active sites of these enzymes, but no three-dimensional
(3D) structural evidence is yet available to elucidate the subdomain arrangement and molecular mechanism of catalysis. Based on a
combined sequence and secondary structure alignment against known crystal structures of segments from closely related proteins, we
propose here the 3D model of an N-terminal domain essential for the sucrose binding and splitting in GtfB. A Tim-barrel of (K/L)8
structural characteristics is revealed and the structural correlation for two peptides is described.
Subjects
Glucosyltransferase
Streptococcus mutans
Sucrase activity
Catalytic domain
Three-dimensional model
Tim-barrel
Publisher
臺北市：國立臺灣大學醫學院口腔生物科學研究所
Type
journal article
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