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Glycobiology Advance Access published online on July 24, 2003
Glycobiology, doi:10.1093/glycob/cwg098
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Submitted on April 24, 2003
Revised on June 27, 2003
Accepted on June 27, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

Fold recognition analysis of glycosyltransferases families: further members of structural superfamilies

Octávio L. Franco 1* and Daniel J. Rigden 2

1 Embrapa Genetic Resources and Biotechnology, Cenargen/Embrapa, Brasilia-DF, Brazil; Universidade Católica de Brasília, Brasília-DF, Brazil
2 Embrapa Genetic Resources and Biotechnology, Cenargen/Embrapa, Brasilia-DF, Brazil

* To whom correspondence should be addressed. E-mail: ocfranco{at}cenargen.embrapa.br.

Abstract

Glycosyltransferases (GTs) are diverse enzymes organized into 65 families. X-ray crystallography and in silico studies have shown many of these to belong to two structural superfamilies - GT-A and GT-B. Here we demonstrate, through application of fold recognition and iterated sequence searches, that families 60, 62 and 64 may also be grouped into the GT-A fold superfamily. Analysis of conserved acidic residues suggests that catalytic sites are better conserved in superfamily GT-B than in GT-A. Although 26% and 29% of GT families may now be confidently placed in superfamilies GT-A and GT-B, respectively, the remaining 45% of families bear no discernible resemblance to either superfamily which, given the sensitivity of modern fold recognition methods, suggests the existence of novel structural scaffolds associated with GT activity. Furthermore, bioinformatics studies indicate the apparent ease with which mechanism - inverting or retaining - may change during evolution.


glycosyltransferases, MurG, SpsA, fold recognition, evolutionary relationships
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