5DMA

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

Summary for 5DMA

• Entry DOI: 10.2210/pdb5dma/pdb
• Descriptor: ATP-dependent DNA helicase PcrA (2 entities in total)
• Functional Keywords: rna polymerase, pcra/uvrd helicase, tudor domain, transcription, hydrolase
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 1
• Total formula weight: 5977.88

Authors

Lin, C.L.,Dillingham, M.,Wigley, D. (deposition date: 2015-09-08, release date: 2016-09-28, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.53 Å)