| Literature DB >> 16037492 |
Christelle Breton1, Lenka Snajdrová, Charlotte Jeanneau, Jaroslav Koca, Anne Imberty.
Abstract
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.Entities:
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Year: 2005 PMID: 16037492 DOI: 10.1093/glycob/cwj016
Source DB: PubMed Journal: Glycobiology ISSN: 0959-6658 Impact factor: 4.313