1ENY
CRYSTAL STRUCTURE AND FUNCTION OF THE ISONIAZID TARGET OF MYCOBACTERIUM TUBERCULOSIS
Summary for 1ENY
| Entry DOI | 10.2210/pdb1eny/pdb |
| Descriptor | ENOYL-ACYL CARRIER PROTEIN (ACP) REDUCTASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, oxidoreductase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 1 |
| Total formula weight | 29056.99 |
| Authors | Dessen, A.,Quemard, A.,Blanchard, J.S.,Jacobs Jr., W.R.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (deposition date: 1995-01-27, release date: 1996-01-29, Last modification date: 2024-02-07) |
| Primary citation | Dessen, A.,Quemard, A.,Blanchard, J.S.,Jacobs Jr., W.R.,Sacchettini, J.C. Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis. Science, 267:1638-1641, 1995 Cited by PubMed Abstract: Resistance to isoniazid in Mycobacterium tuberculosis can be mediated by substitution of alanine for serine 94 in the InhA protein, the drug's primary target. InhA was shown to catalyze the beta-nicotinamide adenine dinucleotide (NADH)-specific reduction of 2-trans-enoyl-acyl carrier protein, an essential step in fatty acid elongation. Kinetic analyses suggested that isoniazid resistance is due to a decreased affinity of the mutant protein for NADH. The three-dimensional structures of wild-type and mutant InhA, refined to 2.2 and 2.7 angstroms, respectively, revealed that drug resistance is directly related to a perturbation in the hydrogen-bonding network that stabilizes NADH binding. PubMed: 7886450PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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