Open AccessPreliminary crystallographic analysis of GpgS, a key glucosyltransferase involved in methylglucose lipopolysaccharide biosynthesis in Mycobacterium tuberculosis
Author(s) -
Gest Petra,
Kaur Devinder,
Pham Ha T.,
Van Der Woerd Mark,
Hansen Emily,
Brennan Patrick J.,
Jackson Mary,
Guerin Marcelo E.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108032892
Subject(s) - lipopolysaccharide , tuberculosis , biosynthesis , microbiology and biotechnology , mycobacterium tuberculosis , key (lock) , chemistry , crystallography , biochemistry , biology , medicine , immunology , gene , ecology , pathology
Glucosyl-3-phosphoglycerate synthase (GpgS) is a key enzyme that catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria. These important molecules are believed to be involved in the regulation of fatty-acid and mycolic acid synthesis. The enzyme belongs to the recently defined GT81 family of retaining glycosyltransferases (CAZy, Carbohydrate-Active Enzymes Database; see http://www.cazy.org). Here, the purification, crystallization and preliminary crystallographic analysis are reported of GpgS from Mycobacterium tuberculosis and of its complex with UDP. GpgS crystals belonged to space group I4, with unit-cell parameters a = 98.85, b = 98.85, c = 127.64 A, and diffracted to 2.6 A resolution. GpgS-UDP complex crystals belonged to space group I4, with unit-cell parameters a = 98.32, b = 98.32, c = 127.96 A, and diffracted to 3.0 A resolution.