5NSR

Cryo-EM structure of RNA polymerase-sigma54 holo enzyme with promoter DNA closed complex

5NSR の概要

• エントリーDOI: 10.2210/pdb5nsr/pdb
• EMDBエントリー: 3695
• 分子名称: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (7 entities in total)
• 機能のキーワード: transcription initiation, rna polymerase, sigma54, transcription
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 490557.16

構造登録者

Glyde, R.,Ye, F.Z.,Darbari, V.C.,Zhang, N.,Buck, M.,Zhang, X.D. (登録日: 2017-04-26, 公開日: 2017-06-28, 最終更新日: 2019-12-11)

主引用文献

Glyde, R.,Ye, F.,Darbari, V.C.,Zhang, N.,Buck, M.,Zhang, X.
Structures of RNA Polymerase Closed and Intermediate Complexes Reveal Mechanisms of DNA Opening and Transcription Initiation.
Mol. Cell, 67:106-116.e4, 2017

PubMed Abstract: Gene transcription is carried out by RNA polymerases (RNAPs). For transcription to occur, the closed promoter complex (RPc), where DNA is double stranded, must isomerize into an open promoter complex (RPo), where the DNA is melted out into a transcription bubble and the single-stranded template DNA is delivered to the RNAP active site. Using a bacterial RNAP containing the alternative σ factor and cryoelectron microscopy, we determined structures of RPc and the activator-bound intermediate complex en route to RPo at 3.8 and 5.8 Å. Our structures show how RNAP-σ interacts with promoter DNA to initiate the DNA distortions required for transcription bubble formation, and how the activator interacts with RPc, leading to significant conformational changes in RNAP and σ that promote RPo formation. We propose that DNA melting is an active process initiated in RPc and that the RNAP conformations of intermediates are significantly different from that of RPc and RPo.

PubMed: 28579332
DOI: 10.1016/j.molcel.2017.05.010

実験手法

ELECTRON MICROSCOPY (3.8 Å)