1i6v
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(New page: 200px<br /><applet load="1i6v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i6v, resolution 3.3Å" /> '''THERMUS AQUATICUS COR...)
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Revision as of 14:59, 20 November 2007
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THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX
Overview
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.
About this Structure
1I6V is a Protein complex structure of sequences from Thermus aquaticus with MG, ZN and RFP as ligands. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.
Reference
Structural mechanism for rifampicin inhibition of bacterial rna polymerase., Campbell EA, Korzheva N, Mustaev A, Murakami K, Nair S, Goldfarb A, Darst SA, Cell. 2001 Mar 23;104(6):901-12. PMID:11290327
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