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Substrate-induced conformational changes in glycosyltransferases.
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Substrate-induced conformational changes in glycosyltransferases.

Author: PK Qasba Affiliation: Structural Glycobiology Section, Laboratory of Experimental and Computational Biology, CCR, NCI-Frederick, MD 21702, USA. qsaba@helix.nih.gov; B Ramakrishnan; E Boeggeman
Edition/Format: Article Article : English
Publication:Trends in biochemical sciences, 2005 Jan; 30(1): 53-62
Database:From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
Other Databases: British Library Serials
Summary:
Oligosaccharide chains of glycoproteins, glycolipids and glycosaminoglycans are synthesized by glycosyltransferases by the transfer of specific glycosyl moieties from activated sugar-nucleotide donors to specific acceptors. Structural studies on several of these enzymes have shown that one or two flexible loops at the substrate-binding site of the enzymes undergo a marked conformational change from an open to a  Read more...
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Document Type: Article
All Authors / Contributors: PK Qasba Affiliation: Structural Glycobiology Section, Laboratory of Experimental and Computational Biology, CCR, NCI-Frederick, MD 21702, USA. qsaba@helix.nih.gov; B Ramakrishnan; E Boeggeman
ISSN:0968-0004
Language Note: English
Unique Identifier: 110328847
Awards:

Abstract:

Oligosaccharide chains of glycoproteins, glycolipids and glycosaminoglycans are synthesized by glycosyltransferases by the transfer of specific glycosyl moieties from activated sugar-nucleotide donors to specific acceptors. Structural studies on several of these enzymes have shown that one or two flexible loops at the substrate-binding site of the enzymes undergo a marked conformational change from an open to a closed conformation on binding the donor substrate. This conformational change, in which the loop acts as a lid covering the bound donor substrate, creates an acceptor-binding site. After the glycosyl unit is transferred from the donor to the acceptor, the saccharide product is ejected and the loop reverts to its native conformation, thereby releasing the remaining nucleotide moiety. The specificity of the sugar donor is determined by a few residues in the sugar-nucleotide-binding pocket of the enzyme that are conserved among the family members from different species.

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