Tsai, Yau WeiYau WeiTsaiJEAN-SAN CHIAShiau, Yuh YuanYuh YuanShiauChou, Hsiu ChuanHsiu ChuanChouLiaw, Yen ChywanYen ChywanLiawKUO-LONG LOU2023-01-162023-01-162000-07-0103781097https://scholars.lib.ntu.edu.tw/handle/123456789/627292Glucosyltransferases (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. Copyright (C) 2000 Federation of European Microbiological Societies.enCatalytic domain | Glucosyltransferase | Streptococcus mutans | Sucrase activity | Three-dimensional model | Tim-barreljournal article10.1016/S0378-1097(00)00213-5108672372-s2.0-0034237711https://api.elsevier.com/content/abstract/scopus_id/0034237711