Expression, purification, crystallization and preliminary X-ray characterization of a putative glycosyltransferase of the GT-A fold found in mycobacteria

Zara Jennifer Fulton, Paul Crellin, Rajini Brammananth, Leyla Zaker-Tabrizi, Ross Leon Coppel, Jamie Rossjohn, Travis Clarke Beddoe

Research output: Contribution to journalArticleResearchpeer-review

6 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)428 - 431
Number of pages4
JournalActa Crystallographica Section F: Structural Biology Communications
Issue numberPt 5
Publication statusPublished - 2008

Cite this