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Substrate-induced conformational changes in glycosyltransferases. | LitMetric

Substrate-induced conformational changes in glycosyltransferases.

Trends Biochem Sci

Structural Glycobiology Section, Laboratory of Experimental and Computational Biology, CCR, NCI-Frederick, MD 21702, USA.

Published: January 2005

AI Article Synopsis

  • * Structural studies reveal that flexible loops in these enzymes change shape significantly when the donor substrate binds, transitioning from an open to a closed conformation that helps create a site for the acceptor.
  • * The specificity of the sugar donors is primarily determined by a few conserved residues in the sugar-nucleotide-binding pocket of the enzyme, which can vary across different species.

Article 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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Source
http://dx.doi.org/10.1016/j.tibs.2004.11.005DOI Listing

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