8IGR

Cryo-EM structure of CII-dependent transcription activation complex

8IGR の概要

• エントリーDOI: 10.2210/pdb8igr/pdb
• EMDBエントリー: 35438
• 分子名称: DNA-directed RNA polymerase subunit alpha, ZINC ION, DNA-directed RNA polymerase subunit beta, ... (10 entities in total)
• 機能のキーワード: rna polymerase, transcription, transcription activation, bacteriophage, cii
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 556775.21

構造登録者

Zhao, M.,Gao, B.,Wen, A.,Feng, Y.,Lu, Y. (登録日: 2023-02-21, 公開日: 2023-05-17, 最終更新日: 2023-08-16)

主引用文献

Zhao, M.,Gao, B.,Wen, A.,Feng, Y.,Lu, Y.Q.
Structural basis of lambda CII-dependent transcription activation.
Structure, 31:968-, 2023

PubMed Abstract: The CII protein of bacteriophage λ activates transcription from the phage promoters P, P, and P by binding to two direct repeats that straddle the promoter -35 element. Although genetic, biochemical, and structural studies have elucidated many aspects of λCII-mediated transcription activation, no precise structure of the transcription machinery in the process is available. Here, we report a 3.1-Å cryo-electron microscopy (cryo-EM) structure of an intact λCII-dependent transcription activation complex (TAC-λCII), which comprises λCII, E. coli RNAP-σ holoenzyme, and the phage promoter P. The structure reveals the interactions between λCII and the direct repeats responsible for promoter specificity and the interactions between λCII and RNAP α subunit C-terminal domain responsible for transcription activation. We also determined a 3.4-Å cryo-EM structure of an RNAP-promoter open complex (RPo-P) from the same dataset. Structural comparison between TAC-λCII and RPo-P provides new insights into λCII-dependent transcription activation.

PubMed: 37269829
DOI: 10.1016/j.str.2023.05.008

実験手法

ELECTRON MICROSCOPY (3.1 Å)