6N62

Escherichia coli RNA polymerase sigma70-holoenzyme bound to upstream fork promoter DNA

6N62 の概要

• エントリーDOI: 10.2210/pdb6n62/pdb
• 分子名称: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (9 entities in total)
• 機能のキーワード: complex, rna polymerase, transferase-dna complex, transferase/dna
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 456360.56

構造登録者

Braffman, N.,Hauver, J.,Campbell, E.A.,Darst, S.A. (登録日: 2018-11-24, 公開日: 2019-01-09, 最終更新日: 2024-10-23)

主引用文献

Braffman, N.R.,Piscotta, F.J.,Hauver, J.,Campbell, E.A.,Link, A.J.,Darst, S.A.
Structural mechanism of transcription inhibition by lasso peptides microcin J25 and capistruin.
Proc. Natl. Acad. Sci. U.S.A., 116:1273-1278, 2019

PubMed Abstract: We report crystal structures of the antibacterial lasso peptides microcin J25 (MccJ25) and capistruin (Cap) bound to their natural enzymatic target, the bacterial RNA polymerase (RNAP). Both peptides bind within the RNAP secondary channel, through which NTP substrates enter the RNAP active site, and sterically block trigger-loop folding, which is essential for efficient catalysis by the RNAP. MccJ25 binds deep within the secondary channel in a manner expected to interfere with NTP substrate binding, explaining the partial competitive mechanism of inhibition with respect to NTPs found previously [Mukhopadhyay J, Sineva E, Knight J, Levy RM, Ebright RH (2004) 14:739-751]. The Cap binding determinant on RNAP overlaps, but is not identical to, that of MccJ25. Cap binds further from the RNAP active site and does not sterically interfere with NTP binding, and we show that Cap inhibition is partially noncompetitive with respect to NTPs. This work lays the groundwork for structure determination of other lasso peptides that target the bacterial RNAP and provides a structural foundation to guide lasso peptide antimicrobial engineering approaches.

PubMed: 30626643
DOI: 10.1073/pnas.1817352116

実験手法

X-RAY DIFFRACTION (3.803 Å)