6VSX

X-ray crystal structure of the C-terminal domain of Bacillus subtilis RNA polymerase binding helicase HelD

6VSX の概要

• エントリーDOI: 10.2210/pdb6vsx/pdb
• 分子名称: DNA helicase, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: rna polymerase, helicase, transcription
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21376.33

構造登録者

Murakami, K.S.,Chon, U. (登録日: 2020-02-12, 公開日: 2020-06-10, 最終更新日: 2024-03-06)

主引用文献

Kouba, T.,Koval', T.,Sudzinova, P.,Pospisil, J.,Brezovska, B.,Hnilicova, J.,Sanderova, H.,Janouskova, M.,Sikova, M.,Halada, P.,Sykora, M.,Barvik, I.,Novacek, J.,Trundova, M.,Duskova, J.,Skalova, T.,Chon, U.,Murakami, K.S.,Dohnalek, J.,Krasny, L.
Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase.
Nat Commun, 11:6419-6419, 2020

PubMed Abstract: RNA synthesis is central to life, and RNA polymerase (RNAP) depends on accessory factors for recovery from stalled states and adaptation to environmental changes. Here, we investigated the mechanism by which a helicase-like factor HelD recycles RNAP. We report a cryo-EM structure of a complex between the Mycobacterium smegmatis RNAP and HelD. The crescent-shaped HelD simultaneously penetrates deep into two RNAP channels that are responsible for nucleic acids binding and substrate delivery to the active site, thereby locking RNAP in an inactive state. We show that HelD prevents non-specific interactions between RNAP and DNA and dissociates stalled transcription elongation complexes. The liberated RNAP can either stay dormant, sequestered by HelD, or upon HelD release, restart transcription. Our results provide insights into the architecture and regulation of the highly medically-relevant mycobacterial transcription machinery and define HelD as a clearing factor that releases RNAP from nonfunctional complexes with nucleic acids.

PubMed: 33339823
DOI: 10.1038/s41467-020-20158-4

実験手法

X-RAY DIFFRACTION (2 Å)