Structural Mechanism for Rifampicin Inhibition of Bacterial RNA Polymerase

@article{Campbell2001StructuralMF,
  title={Structural Mechanism for Rifampicin Inhibition of Bacterial RNA Polymerase},
  author={Elizabeth A. Campbell and Nataliya Korzheva and Arkady Mustaev and Katsuhiko S. Murakami and Satish K. Nair and Alexander Goldfarb and Seth A. Darst},
  journal={Cell},
  year={2001},
  volume={104},
  pages={901-912}
}
Rifampicin (Rif) is one of the most potent and broad spectrum antibiotics against bacterial pathogens and is a key component of anti-tuberculosis therapy, stemming from its inhibition of the bacterial RNA polymerase (RNAP). We determined the crystal structure of Thermus aquaticus core RNAP complexed with Rif. The inhibitor binds in a pocket of the RNAP beta subunit deep within the DNA/RNA channel, but more than 12 A away from the active site. The structure, combined with biochemical results… Expand

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