Glycosidic bond formation is a ubiquitous enzyme-catalysed reaction. This glycosyltransferase-mediated process is responsible for the biosynthesis of innumerable oligosaccharides and glycoconjugates and is often organism- or cell-specific. However, despite the abundance of genomic information on glycosyltransferases (GTs), there is a lack of structural data for this versatile class of enzymes. Here, the cloning, expression, purification and crystallization of an essential 329-amino-acid (34.8 kDa) putative GT of the classic GT-A fold implicated in mycobacterial cell-wall biosynthesis are reported. Crystals of MAP2569c from Mycobacterium avium subsp. paratuberculosis were grown in 1.6 M monoammonium dihydrogen phosphate and 0.1 M sodium citrate pH 5.5. A complete data set was collected to 1.8 A resolution using synchrotron radiation from a crystal belonging to space group P4(1)2(1)2.
|Pages (from-to)||428 - 431|
|Number of pages||4|
|Journal||Acta Crystallographica. Section F: Structural Biology Communications|
|Issue number||Pt 5|
|Publication status||Published - 2008|
Fulton, Z. J., Crellin, P., Brammananth, R., Zaker-Tabrizi, L., Coppel, R. L., Rossjohn, J., & Beddoe, T. C. (2008). Expression, purification, crystallization and preliminary X-ray characterization of a putative glycosyltransferase of the GT-A fold found in mycobacteria. Acta Crystallographica. Section F: Structural Biology Communications, 64(Pt 5), 428 - 431.