3C48
Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure.
Summary for 3C48
| Entry DOI | 10.2210/pdb3c48/pdb |
| Descriptor | Predicted glycosyltransferases, SULFATE ION (3 entities in total) |
| Functional Keywords | retaining glycosyltransferase, beta alpha beta, substrate assisted catalysis, transferase |
| Biological source | Corynebacterium glutamicum |
| Total number of polymer chains | 2 |
| Total formula weight | 96553.68 |
| Authors | Vetting, M.W.,Frantom, P.A.,Blanchard, J.S. (deposition date: 2008-01-29, release date: 2008-03-25, Last modification date: 2024-02-21) |
| Primary citation | Vetting, M.W.,Frantom, P.A.,Blanchard, J.S. Structural and Enzymatic Analysis of MshA from Corynebacterium glutamicum: SUBSTRATE-ASSISTED CATALYSIS J.Biol.Chem., 283:15834-15844, 2008 Cited by PubMed 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 of UDP-N-acetylglucosamine and 1-L-myo-inositol-1-phosphate. Molecular models of the ternary complex suggest a mechanism in which the beta-phosphate of the substrate, UDP-N-acetylglucosamine, promotes the nucleophilic attack of the 3-hydroxyl group of 1-L-myo-inositol-1-phosphate while at the same time promoting the cleavage of the sugar nucleotide bond. PubMed: 18390549DOI: 10.1074/jbc.M801017200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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