Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis.

ABSTRACT: The glycosyltransferase termed MshA catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to 1-L-myo-inositol-1-phosphate in the first committed step of mycothiol biosynthesis. The structure of MshA from Corynebacterium glutamicum was determined both in the absence of substrates and in a complex with UDP and 1-L-myo-inositol-1-phosphate. MshA belongs to the GT-B structural family whose members have a two-domain structure with both domains exhibiting a Rossman-type fold. Binding of the donor sugar to the C-terminal domain produces a 97 degrees rotational reorientation of the N-terminal domain relative to the C-terminal domain, clamping down on UDP and generating the binding site for 1-L-myo-inositol-1-phosphate. The structure highlights the residues important in binding

SUBMITTER: Vetting MW 

PROVIDER: S-EPMC2414306 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature