3VW0

Crystal Structure of The Dequalinum-bound Form of RamR (Transcriptional Regulator of TetR Family) From Salmonella Typhimurium

Summary for 3VW0

• Entry DOI: 10.2210/pdb3vw0/pdb
• Related: 3VVX 3VVY 3VVZ 3VW1 3VW2
• Descriptor: Putative regulatory protein, SULFATE ION, DEQUALINIUM, ... (4 entities in total)
• Functional Keywords: tetr transcriptional regulator family, hth-motif, transcriptional regulator, dna binding, transcription regulator
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 4
• Total formula weight: 89474.63

Authors

Sakurai, K.,Yamasaki, S.,Nakashima, R.,Nikaido, E.,Yamaguchi, A.,Nishino, K. (deposition date: 2012-07-30, release date: 2013-07-03, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)