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Abstract
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, explains
the effects of Rif on RNAP function and indicates that the inhibitor acts by directly
blocking the path of the elongating RNA when the transcript becomes 2 to 3 nt in length.