Crystal structure of a UDP-glucose-specific glycosyltransferase from a Mycobacterium species

Zara Jennifer Fulton, Adrian Dale McAlister, Matthew CJ Wilce, Rajini Brammananth, Leyla Zaker-Tabrizi, Matthew Anthony Perugini, Stephen Paul Bottomley, Ross Leon Coppel, Paul Crellin, Jamie Rossjohn, Travis Clarke Beddoe

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23 Citations (Scopus)


Glycosyltransferases (GTs) are a large and ubiquitous family of enzymes that specifically transfer sugar moieties to a range of substrates. Mycobacterium tuberculosis contains a large number of GTs, many of which are implicated in cell wall synthesis, yet the majority of these GTs remain poorly characterized. Here, we report the high-resolution crystal structures of an essential GT (MAP2569c) from Mycobacterium avium subsp. paratuberculosis (a close homologue of Rv1208 from M. tuberculosis) in its apo- and ligand-bound forms. The structure adopted the GT-A fold and possessed the characteristic D-x-D motif that coordinated a Mn2+ ion. Atypical of most GTs characterised to date, MAP2569c exhibited specificity towards the donor substrate, UDP-glucose. The structure of this ligated complex revealed an induced-fit binding mechanism and provided a basis for this unique specificity. Collectively, the structural features suggested MAP2569c adopted a retaining enzymatic mechanism, which has implications for the classification of other GTs in this large superfamily.
Original languageEnglish
Pages (from-to)27881 - 27890
Number of pages10
JournalJournal of Biological Chemistry
Issue number41
Publication statusPublished - 2008

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