1V35
Crystal Structure of Eoyl-ACP Reductase with NADH
Summary for 1V35
| Entry DOI | 10.2210/pdb1v35/pdb |
| Related | 1UH5 |
| Descriptor | enoyl-ACP reductase, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | fabi, nadh, enoyl-acp reductase, p.falciparum, oxidoreductase |
| Biological source | Plasmodium falciparum (malaria parasite P. falciparum) |
| Total number of polymer chains | 2 |
| Total formula weight | 75819.25 |
| Authors | SwarnaMukhi, P.L.,Kapoor, M.,surolia, N.,Surolia, A.,Suguna, K. (deposition date: 2003-10-28, release date: 2004-09-28, Last modification date: 2023-10-25) |
| Primary citation | Pidugu, L.S.,Kapoor, M.,Surolia, N.,Surolia, A.,Suguna, K. Structural basis for the variation in triclosan affinity to enoyl reductases. J.Mol.Biol., 343:147-155, 2004 Cited by PubMed Abstract: Bacteria synthesize fatty acids in a dissociated type pathway different from that in humans. Enoyl acyl carrier protein reductase, which catalyzes the final step of fatty acid elongation, has been validated as a potential anti-microbial drug target. Triclosan is known to inhibit this enzyme effectively. Precise characterization of the mode of triclosan binding is required to develop highly specific inhibitors. With this in view, interactions between triclosan, the cofactor NADH/NAD+ and the enzyme from five different species, one plant and four of microbial origin, have been examined in the available crystal structures. A comparison of these structures shows major structural differences at the substrate/inhibitor/cofactor-binding loop. The analysis reveals that the conformation of this flexible loop and the binding affinities of triclosan to each of these enzymes are strongly correlated. PubMed: 15381426DOI: 10.1016/j.jmb.2004.08.033 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report
