Knowledge‐based model of a glucosyltransferase from the oral bacterial group of mutans streptococci
Open Access
- 31 December 1997
- journal article
- research article
- Published by Wiley in Protein Science
- Vol. 6 (12), 2489-2493
- https://doi.org/10.1002/pro.5560061201
Abstract
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 α‐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 α‐amylases and glucosyltransferase from Streptococcus downei gtfI (GTF). The significance of GTF similarity is underlined by GTF/α‐amylase residues conserved in all but one α‐amylase invariant residues. Site‐directed mutagenesis of the three GTF catalytic residues are homologous with the α‐amylase catalytic triad. The glucosyltransferases are members of the 4/7‐superfamily that have a (β/α)8‐barrel structure and belong to family 13 of the glycohydralases.Keywords
This publication has 43 references indexed in Scilit:
- A circularly permuted α‐amylase‐type α/β‐barrel structure in glucan‐synthesizing glucosyltransferasesFEBS Letters, 1996
- The structure of human pancreaticα-amylase at 1.8 Å resolution and comparisons with related enzymesProtein Science, 1995
- β‐Glucosidase, β‐galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes wit 8‐fold β/α architecture and with two conserved glutamates near the carboxy‐terminal ends of β‐strands four and sevenFEBS Letters, 1995
- Parallel β/α‐barrels of α‐amylase, cyclodextrin glycosyltransferase and oligo‐1,6‐glucosidase versus the barrel of β‐amylase: Evolutionary distance is a reflection of unrelated sequencesFEBS Letters, 1994
- Crystal and Molecular Structure of Barley α-AmylaseJournal of Molecular Biology, 1994
- Nucleotide Sequence and X-ray Structure of Cyclodextrin Glycosyltransferase from Bacillus circulans Strain 251 in a Maltose-dependent Crystal FormJournal of Molecular Biology, 1994
- Refined Molecular Structure of Pig Pancreatic α-Amylase at 2·1 Å ResolutionJournal of Molecular Biology, 1994
- Analysis of the catalytic center of Cyclomaltodextrinase from Thermoanaerobacter ethanolicus 39EFEBS Letters, 1993
- Functional relationships between cyclodextrin glucanotransferase from an alkalophilic Bacillus and α‐amylases Site‐directed mutagenesis of the conserved two Asp and one Glu residuesFEBS Letters, 1992
- Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolutionJournal of Molecular Biology, 1991