Protein Science, Vol 6, Issue 12 2489-2493, Copyright © 1997 by Cold Spring Harbor Laboratory Press

ARTICLE

Knowledge-based model of a glucosyltransferase from the oral bacterial group of mutans streptococci

K. S. DEVULAPALLE, S. D. GOODMAN, Q. GAO, A. HEMSLEY and G. MOOSER
Department of Basic Sciences, School of Dentistry, University of Southern California, Los Angeles, California 90089-0641

Mutans streptococci glucosyltransferases catalyze glucosyl transfer from sucrose to a glucan chain. We previously identified an aspartyl residue that participates in stabilizing the glucosyl transition state. The sequence surrounding the aspartate was found to have substantial sequence similarity with members of {alpha}-amylase family. Because little is known of the protein structure beyond the amino acid sequence, we used a knowledge-based interactive algorithm, MACAW, which provided significant level of homology with {alpha}-amylases and glucosyltransferase from Streptococcus downei gtfI (GTF). The significance of GTF similarity is underlined by GTF/{alpha}-amylase residues conserved in all but one {alpha}-amylase invariant residues. Site-directed mutagenesis of the three GTF catalytic residues are homologous with the {alpha}-amylase catalytic triad. The glucosyltransferases are members of the 4/7-superfamily that have a ({beta}/{alpha})(8)-barrel structure and belong to family 13 of the glycohydralases.
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