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Glycobiology Advance Access originally published online on July 21, 2005
Glycobiology 2006 16(2):29R-37R; doi:10.1093/glycob/cwj016
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org

REVIEW

Structures and mechanisms of glycosyltransferases

Christelle Breton1,2, Lenka Snajdrová2,3, Charlotte Jeanneau2, Jaroslav Koca3 and Anne Imberty1,2

2 CERMAV–CNRS, affiliated with Université Joseph Fourier, PO Box 53, 38041 Grenoble cedex 9, France; and 3 NCBR, Masaryk University, Kotlarska 2, CZ-611 37 Brno, Czech Republic


1 To whom correspondence should be addressed; e-mail: breton{at}cermav.cnrs.fr and imberty{at}cermav.cnrs.fr

Glycosyltransferases (GTs) catalyze the transfer of a sugar moiety from an activated donor sugar onto saccharide and nonsaccharide acceptors. A sequence-based classification spreads GTs in many families thus reflecting the variety of molecules that can be used as acceptors. In contrast, this enzyme family is characterized by a more conserved three-dimensional architecture. Until recently, only two different folds (GT-A and GT-B) have been identified for solved crystal structures. The recent report of a structure for a bacterial sialyltransferase allows the definition of a new fold family. Progress in the elucidation of the structures and mechanisms of GTs are discussed in this review. To accommodate the growing number of crystal structures, we created the 3D-Glycosyltransferase database to gather structural information concerning this class of enzymes.

Key words: fold recognition / glycosyltransferase / mechanism / superfamily / three-dimensional structure


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