1V35
Crystal Structure of Eoyl-ACP Reductase with NADH
1V35 の概要
エントリーDOI | 10.2210/pdb1v35/pdb |
関連するPDBエントリー | 1UH5 |
分子名称 | enoyl-ACP reductase, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE (3 entities in total) |
機能のキーワード | fabi, nadh, enoyl-acp reductase, p.falciparum, oxidoreductase |
由来する生物種 | Plasmodium falciparum (malaria parasite P. falciparum) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 75819.25 |
構造登録者 | SwarnaMukhi, P.L.,Kapoor, M.,surolia, N.,Surolia, A.,Suguna, K. (登録日: 2003-10-28, 公開日: 2004-09-28, 最終更新日: 2023-10-25) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.5 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
