Open AccessThree‐dimensional modelling of the catalytic domain of Streptococcus mutans glucosyltransferase GtfB
Author(s) -
Tsai YauWei,
Chia JeanShan,
Shiau YuhYuan,
Chou HsiuChuan,
Liaw YenChywan,
Lou KuoLong
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09171.x
Subject(s) - glucosyltransferase , streptococcus mutans , glucosyltransferases , chemistry , biochemistry , hydrolase , enzyme , biology , bacteria , genetics
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 (α/β) 8 structural characteristics is revealed and the structural correlation for two peptides is described.