6WVJ

Cryo-EM structure of Bacillus subtilis RNA Polymerase elongation complex

6WVJ の概要

• エントリーDOI: 10.2210/pdb6wvj/pdb
• 関連するPDBエントリー: 6WVK
• EMDBエントリー: 21920
• 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: dna-dependent rna polymerase, transcription, transcription-dna-rna complex, transcription/dna/rna
• 由来する生物種: Bacillus subtilis (strain 168); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 357310.03

構造登録者

Newing, T.,Tolun, G.,Oakley, A.J. (登録日: 2020-05-06, 公開日: 2020-11-18, 最終更新日: 2024-05-29)

主引用文献

Newing, T.P.,Oakley, A.J.,Miller, M.,Dawson, C.J.,Brown, S.H.J.,Bouwer, J.C.,Tolun, G.,Lewis, P.J.
Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD.
Nat Commun, 11:6420-6420, 2020

PubMed Abstract: In bacteria, transcription complexes stalled on DNA represent a major source of roadblocks for the DNA replication machinery that must be removed in order to prevent damaging collisions. Gram-positive bacteria contain a transcription factor HelD that is able to remove and recycle stalled complexes, but it was not known how it performed this function. Here, using single particle cryo-electron microscopy, we have determined the structures of Bacillus subtilis RNA polymerase (RNAP) elongation and HelD complexes, enabling analysis of the conformational changes that occur in RNAP driven by HelD interaction. HelD has a 2-armed structure which penetrates deep into the primary and secondary channels of RNA polymerase. One arm removes nucleic acids from the active site, and the other induces a large conformational change in the primary channel leading to removal and recycling of the stalled polymerase, representing a novel mechanism for recycling transcription complexes in bacteria.

PubMed: 33339820
DOI: 10.1038/s41467-020-20157-5

実験手法

ELECTRON MICROSCOPY (3.36 Å)