5DAJ
Crystal structure of NalD, the secondary repressor of MexAB-OprM multidrug efflux pump in Pseudomonas aeruginosa
5DAJ の概要
| エントリーDOI | 10.2210/pdb5daj/pdb |
| 分子名称 | NalD (2 entities in total) |
| 機能のキーワード | repressor, transcriptional regulator, tetr family, transcription regulator |
| 由来する生物種 | Pseudomonas aeruginosa PAO1 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 198683.92 |
| 構造登録者 | Chen, W.Z.,Wang, D.,Huang, S.Q.,Hu, Q.Y.,Liu, X.C.,Gan, J.H.,Chen, H. (登録日: 2015-08-20, 公開日: 2016-04-20, 最終更新日: 2024-10-16) |
| 主引用文献 | Chen, W.Z.,Wang, D.,Zhou, W.,Sang, H.,Liu, X.C.,Ge, Z.,Zhang, J.,Lan, L.,Yang, C.G.,Chen, H. Novobiocin binding to NalD induces the expression of the MexAB-OprM pump in Pseudomonas aeruginosa Mol.Microbiol., 100:749-758, 2016 Cited by PubMed Abstract: NalD was reported to be the secondary repressor of the MexAB-OprM multidrug efflux pump, the major system contributing to intrinsic multidrug resistance in Pseudomonas aeruginosa. Here, we show that novobiocin binds directly to NalD, which leads NalD to dissociate from the DNA promoter, and thus de-represses the expression of the MexAB-OprM pump. In addition, we have solved the crystal structure of NalD at a resolution of 2.90 Å. The structural alignment of NalD to its homologue TtgR reveals that the residues N129 and H167 in NalD are involved in its novobiocin-binding ability. We have confirmed the function of these two amino acids by EMSA and plate assay. The results presented here highlight the importance and diversity of regulatory mechanism in bacterial antibiotic resistance, and provide further insight for novel antimicrobial development. PubMed: 26844397DOI: 10.1111/mmi.13346 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.65 Å) |
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