3VW2

Crystal Strucuture of The Berberine-bound Form of RamR (Transcriptional Regurator of TetR Family) from Salmonella Typhimurium

3VW2 の概要

• エントリーDOI: 10.2210/pdb3vw2/pdb
• 関連するPDBエントリー: 3VVX 3VVY 3VVZ 3VW0 3VW1
• 分子名称: Putative regulatory protein, BERBERINE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: tetr transcriptional regulator family, hth-motif, transcriptional regulator, dna binding, transcription regulator
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 89906.74

構造登録者

Sakurai, K.,Nikaido, E.,Nakashima, R.,Yamasaki, S.,Yamaguchi, A.,Nishino, K. (登録日: 2012-07-30, 公開日: 2013-07-03, 最終更新日: 2024-03-20)

主引用文献

Yamasaki, S.,Nikaido, E.,Nakashima, R.,Sakurai, K.,Fujiwara, D.,Fujii, I.,Nishino, K.
The crystal structure of multidrug-resistance regulator RamR with multiple drugs
Nat Commun, 4:2078-2078, 2013

PubMed Abstract: RamR is a transcriptional repressor of the gene-encoding RamA protein, which controls the expression of the multidrug efflux system genes acrAB-tolC. RamR is an important multidrug-resistance factor, however, its structure and the identity of the molecules to which it responds have been unknown. Here, we report the crystal structure of RamR in complex with multiple drugs, including berberine, crystal violet, dequalinium, ethidium bromide and rhodamine 6G. All compounds are found to interact with Phe155 of RamR, and each compound is surrounded by different amino acid residues. Binding of these compounds to RamR reduces its DNA-binding affinity, which results in the increased expression of ramA. Our results reveal significant flexibility in the substrate-recognition region of RamR, which regulates the bacterial efflux participating in multidrug resistance.

PubMed: 23800819
DOI: 10.1038/ncomms3078

実験手法

X-RAY DIFFRACTION (2.34 Å)