2XW7
Structure of Mycobacterium smegmatis putative reductase MS0308
Summary for 2XW7
| Entry DOI | 10.2210/pdb2xw7/pdb |
| Descriptor | DIHYDROFOLATE REDUCTASE, TETRAETHYLENE GLYCOL, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, nadph |
| Biological source | MYCOBACTERIUM SMEGMATIS |
| Total number of polymer chains | 2 |
| Total formula weight | 41166.18 |
| Authors | Evangelopoulos, D.,Gupta, A.,Lack, N.,Cronin, N.,Daviter, T.,Sim, E.,Keep, N.H.,Bhakta, S. (deposition date: 2010-11-01, release date: 2010-12-01, Last modification date: 2024-11-20) |
| Primary citation | Evangelopoulos, D.,Cronin, N.,Daviter, T.,Sim, E.,Keep, N.H.,Bhakta, S. Characterization of an Oxidoreductase from the Arylamine N-Acetyltransferase Operon in Mycobacterium Smegmatis. FEBS J., 278:4824-, 2011 Cited by PubMed Abstract: Mycobacterium tuberculosis, the most successful bacterial pathogen, causes tuberculosis, a disease that still causes more than 2 million deaths per year. Arylamine N-acetyltransferase is an enzyme that is conserved in most Mycobacterium spp. The nat gene belongs to an operon that is important for the intracellular survival of M. tuberculosis within macrophages. The nat operon in Mycobacterium smegmatis and other fast-growing mycobacterial species has a unique organization containing genes with uncharacterized function. Here, we describe the biochemical, biophysical and structural characterization of the MSMEG_0308 gene product (MS0308) of the M. smegmatis nat operon. While characterizing the function of MS0308, we validated the oxidoreductase property; however, we found that the enzyme was not utilizing dihydrofolate as its substrate, hence we first report that MS0308 is not a dihydrofolate reductase, as annotated in the genome. The structure of this oxidoreductase was solved at 2.0 Å in complex with the cofactor NADPH and has revealed the hydrophobic pocket where the endogenous substrate binds. PubMed: 21972977DOI: 10.1111/J.1742-4658.2011.08382.X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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