1i6v

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{{STRUCTURE_1i6v| PDB=1i6v | SCENE= }}
{{STRUCTURE_1i6v| PDB=1i6v | SCENE= }}
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'''THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX'''
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===THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11290327 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11290327}}
==About this Structure==
==About this Structure==
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[[Category: Transcription]]
[[Category: Transcription]]
[[Category: Transferase]]
[[Category: Transferase]]
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Revision as of 07:30, 1 July 2008

Image:1i6v.png

Template:STRUCTURE 1i6v

THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX

Template:ABSTRACT PUBMED 11290327

About this Structure

1I6V is a Protein complex structure of sequences from Thermus aquaticus. 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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