6B6H

The cryo-EM structure of a bacterial class I transcription activation complex

6B6H の概要

• エントリーDOI: 10.2210/pdb6b6h/pdb
• EMDBエントリー: 7059 7060
• 分子名称: DNA-directed RNA polymerase subunit alpha, NASCENT RNA 3-MER, ZINC ION, ... (13 entities in total)
• 機能のキーワード: transcription, rna polymerase, catabolite activator protein, camp, transcription-transferase-dna-rna complex, transcription/transferase/dna/rna
• 由来する生物種: Escherichia coli O157:H7; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 573751.36

構造登録者

Liu, B.,Hong, C.,Huang, R.,Yu, Z.,Steitz, T.A. (登録日: 2017-10-02, 公開日: 2017-11-15, 最終更新日: 2024-03-13)

主引用文献

Liu, B.,Hong, C.,Huang, R.K.,Yu, Z.,Steitz, T.A.
Structural basis of bacterial transcription activation.
Science, 358:947-951, 2017

PubMed Abstract: In bacteria, the activation of gene transcription at many promoters is simple and only involves a single activator. The cyclic adenosine 3',5'-monophosphate receptor protein (CAP), a classic activator, is able to activate transcription independently through two different mechanisms. Understanding the class I mechanism requires an intact transcription activation complex (TAC) structure at a high resolution. Here we report a high-resolution cryo-electron microscopy structure of an intact class I TAC containing a CAP dimer, a σ-RNA polymerase (RNAP) holoenzyme, a complete class I CAP-dependent promoter DNA, and a de novo synthesized RNA oligonucleotide. The structure shows how CAP wraps the upstream DNA and how the interactions recruit RNAP. Our study provides a structural basis for understanding how activators activate transcription through the class I recruitment mechanism.

PubMed: 29146813
DOI: 10.1126/science.aao1923

実験手法

ELECTRON MICROSCOPY (3.9 Å)