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Glycobiology Advance Access published online on July 21, 2005

Glycobiology, 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
Received June 3, 2005
Revised July 12, 2005
Accepted July 13, 2005

Review Article

Structures and mechanisms of glycosyltransferases superfamily

Christelle Breton 1*, Lenka Snajdrova 2, Charlotte Jeanneau 1, Jaroslav Koèa 3, and Anne Imberty 1*

1 CERMAV - CNRS, (affiliated with Université Joseph Fourier), BP 53, 38041 Grenoble cedex 9, France
2 CERMAV - CNRS, (affiliated with Université Joseph Fourier), BP 53, 38041 Grenoble cedex 9, France; NCBR, Masaryk University, Kotlarska 2, CZ-611 37 Brno, Czech Republic
3 NCBR, Masaryk University, Kotlarska 2, CZ-611 37 Brno, Czech Republic

* To whom correspondence should be addressed.
Christelle Breton, E-mail: breton{at}cermav.cnrs.fr
Anne Imberty, E-mail: imberty{at}cermav.cnrs.fr


   Abstract

Glycosyltransferases catalyze the transfer of a sugar moiety from an activated donor sugar onto saccharide and non-saccharide acceptors. A sequence-based classification spreads glycosyltransferases in a large number of families thus reflecting the variety of molecules that can be used as acceptors. In contrast, this enzyme family is characterized by a more conserved 3D 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 defination of a new fold family. Progress in the elucidation of the structures and mechanisms of glycosyltransferases are discussed in this review. To accomodate the growing number of crystal structures, the 3D-glycosyltransferase database has been created to gather structural information concerning this class of enzymes.

Keywords: glycosyltransferase/3D structure/fold recognition/classification/mechanism/superfamily.
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