3VVZ
Crystal Strucuture of The Rhodamine 6G-Bound Form of RamR (Transcriptional Regurator of TetR Family) from Salmonella Typhimurium
Summary for 3VVZ
Entry DOI | 10.2210/pdb3vvz/pdb |
Related | 3VVX 3VVY 3VW0 3VW1 3VW2 |
Descriptor | Putative regulatory protein, RHODAMINE 6G, SULFATE ION, ... (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 | 90335.53 |
Authors | Sakurai, K.,Nikaido, E.,Nakashima, R.,Yamasaki, S.,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 Cited by 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: 23800819DOI: 10.1038/ncomms3078 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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