1I6V

THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX

Summary for 1I6V

• Entry DOI: 10.2210/pdb1i6v/pdb
• Related: 1HQM
• Descriptor: DNA-DIRECTED RNA POLYMERASE, RIFAMPICIN, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: transferase, transcription, dna-directed rna polymerase, 3d- structure
• Biological source: Thermus aquaticus; More
• Total number of polymer chains: 5
• Total formula weight: 348330.17

Authors

Campbell, E.A.,Korzheva, N.,Mustaev, A.,Murakami, K.,Goldfarb, A.,Darst, S.A. (deposition date: 2001-03-05, release date: 2001-04-18, Last modification date: 2024-10-30)

Primary citation

Campbell, E.A.,Korzheva, N.,Mustaev, A.,Murakami, K.,Nair, S.,Goldfarb, A.,Darst, S.A.
Structural mechanism for rifampicin inhibition of bacterial rna polymerase.
Cell(Cambridge,Mass.), 104:901-912, 2001

PubMed 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.

PubMed: 11290327
DOI: 10.1016/S0092-8674(01)00286-0

Experimental method

X-RAY DIFFRACTION (3.3 Å)