Toggle Main Menu Toggle Search

Open Access padlockePrints

Insights into the Synthesis of Lipopolysaccharide and Antibiotics through the Structures of Two Retaining Glycosyltransferases from Family GT4

Lookup NU author(s): Dr Mark Proctor, Dr David Bolam, Emeritus Professor Harry Gilbert


Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


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.

Publication metadata

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

Year: 2006

Volume: 13

Issue: 11

Pages: 1143-1152

ISSN (print): 1074-5521

ISSN (electronic): 1879-1301

Publisher: Cell Press


DOI: 10.1016/j.chembiol.2006.09.005

PubMed id: 17113996


Altmetrics provided by Altmetric