5DMA

Crystal structure of C-terminal tudor domain in PcrA/UvrD helicase

5DMA の概要

• エントリーDOI: 10.2210/pdb5dma/pdb
• 分子名称: ATP-dependent DNA helicase PcrA (2 entities in total)
• 機能のキーワード: rna polymerase, pcra/uvrd helicase, tudor domain, transcription, hydrolase
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5977.88

構造登録者

Lin, C.L.,Dillingham, M.,Wigley, D. (登録日: 2015-09-08, 公開日: 2016-09-28, 最終更新日: 2024-05-08)

主引用文献

Sanders, K.,Lin, C.L.,Smith, A.J.,Cronin, N.,Fisher, G.,Eftychidis, V.,McGlynn, P.,Savery, N.J.,Wigley, D.B.,Dillingham, M.S.
The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase.
Nucleic Acids Res., 45:3875-3887, 2017

PubMed Abstract: The PcrA/UvrD helicase functions in multiple pathways that promote bacterial genome stability including the suppression of conflicts between replication and transcription and facilitating the repair of transcribed DNA. The reported ability of PcrA/UvrD to bind and backtrack RNA polymerase (1,2) might be relevant to these functions, but the structural basis for this activity is poorly understood. In this work, we define a minimal RNA polymerase interaction domain in PcrA, and report its crystal structure at 1.5 Å resolution. The domain adopts a Tudor-like fold that is similar to other RNA polymerase interaction domains, including that of the prototype transcription-repair coupling factor Mfd. Removal or mutation of the interaction domain reduces the ability of PcrA/UvrD to interact with and to remodel RNA polymerase complexes in vitro. The implications of this work for our understanding of the role of PcrA/UvrD at the interface of DNA replication, transcription and repair are discussed.

PubMed: 28160601
DOI: 10.1093/nar/gkx074

実験手法

X-RAY DIFFRACTION (1.53 Å)