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Lookup NU author(s): Dr Mark Proctor,
Dr David Bolam,
Emeritus Professor Harry Gilbert
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Glycosyltransferases (GTs) catalyze the synthesis of the myriad glycoconjugates that are central to life. One of the largest families is GT4, which contains several enzymes of therapeutic significance, exemplified by WaaG and AviGT4. WaaG catalyses a key step in lipopolysaccharide synthesis, while AviGT4, produced by Streptomyces viridochromogenes, contributes to the synthesis of the antibiotic avilamycin A. Here we present the crystal structure of both WaaG and AviGT4. The two enzymes contain two "Rossmann-like" (β/α/β) domains characteristic of the GT-B fold. Both recognition of the donor substrate and the catalytic machinery is similar to other retaining GTs that display the GT-B fold. Structural information is discussed with respect to the evolution of GTs and the therapeutic significance of the two enzymes. © 2006 Elsevier Ltd. All rights reserved.
Author(s): Martinez-Fleites C, Proctor MR, Roberts S, Bolam DN, Gilbert HJ, Davies G
Publication type: Article
Publication status: Published
Journal: Chemistry and Biology
ISSN (print): 1074-5521
ISSN (electronic): 1879-1301
Publisher: Cell Press
PubMed id: 17113996
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