4BII
How nature bridges the gap: Crystallographic elucidation of pyridomycin binding to InhA
Summary for 4BII
| Entry DOI | 10.2210/pdb4bii/pdb |
| Related | 4BGE |
| Descriptor | ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH], NICOTINAMIDE-ADENINE-DINUCLEOTIDE, Pyridomycin, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, acp enoyl reductase |
| Biological source | MYCOBACTERIUM TUBERCULOSIS |
| Total number of polymer chains | 4 |
| Total formula weight | 117831.09 |
| Authors | Read, J.A.,Gingell, H. (deposition date: 2013-04-10, release date: 2013-12-04, Last modification date: 2024-05-08) |
| Primary citation | Hartkoorn, R.,Pojer, F.,Read, J.A.,Gingell, H.,Neres, J.,Horlacher, O.,Altmann, K.H.,Cole, S. Pyridomycin Bridges the Nadh and Substrate Binding Pockets of the Enoyl Reductase Inha Nat.Chem.Biol., 10:96-, 2014 Cited by PubMed Abstract: Pyridomycin, a natural product with potent antituberculosis activity, inhibits a major drug target, the InhA enoyl reductase. Here, we unveil the co-crystal structure and unique ability of pyridomycin to block both the NADH cofactor- and lipid substrate-binding pockets of InhA. This is to our knowledge a first-of-a-kind binding mode that discloses a new means of InhA inhibition. Proof-of-principle studies show how structure-assisted drug design can improve the activity of new pyridomycin derivatives. PubMed: 24292073DOI: 10.1038/NCHEMBIO.1405 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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