6BR7
Beryllium fluorinated receiver domain of BfmR from Acinetobacter baumannii
6BR7 の概要
| エントリーDOI | 10.2210/pdb6br7/pdb |
| 関連するPDBエントリー | 5HM6 |
| 分子名称 | BfmR, BERYLLIUM TRIFLUORIDE ION, MAGNESIUM ION, ... (4 entities in total) |
| 機能のキーワード | response regulator, transcription regulator, transcription |
| 由来する生物種 | Acinetobacter baumannii |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 30411.51 |
| 構造登録者 | |
| 主引用文献 | Draughn, G.L.,Milton, M.E.,Feldmann, E.A.,Bobay, B.G.,Roth, B.M.,Olson, A.L.,Thompson, R.J.,Actis, L.A.,Davies, C.,Cavanagh, J. The Structure of the Biofilm-controlling Response Regulator BfmR from Acinetobacter baumannii Reveals Details of Its DNA-binding Mechanism. J. Mol. Biol., 430:806-821, 2018 Cited by PubMed Abstract: The rise of drug-resistant bacterial infections coupled with decreasing antibiotic efficacy poses a significant challenge to global health care. Acinetobacter baumannii is an insidious, emerging bacterial pathogen responsible for severe nosocomial infections aided by its ability to form biofilms. The response regulator BfmR, from the BfmR/S two-component system, is the master regulator of biofilm initiation in A. baumannii and is a tractable therapeutic target. Here we present the structure of A. baumannii BfmR using a hybrid approach combining X-ray crystallography, nuclear magnetic resonance spectroscopy, chemical crosslinking mass spectrometry, and molecular modeling. We also show that BfmR binds the previously proposed bfmRS promoter sequence with moderate affinity. While BfmR shares many traits with other OmpR/PhoB family response regulators, some unusual properties were observed. Most importantly, we observe that when phosphorylated, BfmR binds this promoter sequence with a lower affinity than when not phosphorylated. All other OmpR/PhoB family members studied to date show an increase in DNA-binding affinity upon phosphorylation. Understanding the structural and biochemical mechanisms of BfmR will aid in the development of new antimicrobial therapies. PubMed: 29438671DOI: 10.1016/j.jmb.2018.02.002 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.86 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






