1I6V

THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX

1I6V の概要

• エントリーDOI: 10.2210/pdb1i6v/pdb
• 関連するPDBエントリー: 1HQM
• 分子名称: DNA-DIRECTED RNA POLYMERASE, RIFAMPICIN, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: transferase, transcription, dna-directed rna polymerase, 3d- structure
• 由来する生物種: Thermus aquaticus; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 348330.17

構造登録者

Campbell, E.A.,Korzheva, N.,Mustaev, A.,Murakami, K.,Goldfarb, A.,Darst, S.A. (登録日: 2001-03-05, 公開日: 2001-04-18, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.3 Å)