4DFC

Core UvrA/TRCF complex

4DFC の概要

• エントリーDOI: 10.2210/pdb4dfc/pdb
• 分子名称: Transcription-repair-coupling factor, UvrABC system protein A (2 entities in total)
• 機能のキーワード: alpha/beta domains, dna repair, atp binding, dna binding, nucleotide excision repair, hydrolase-dna binding protein complex, hydrolase/dna binding protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm (By similarity): P0A698
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49083.57

構造登録者

Deaconescu, A.M.,Grigorieff, N. (登録日: 2012-01-23, 公開日: 2012-05-02, 最終更新日: 2023-09-13)

主引用文献

Deaconescu, A.M.,Sevostyanova, A.,Artsimovitch, I.,Grigorieff, N.
Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface.
Proc.Natl.Acad.Sci.USA, 109:3353-3358, 2012

PubMed Abstract: Transcription-coupled DNA repair targets DNA lesions that block progression of elongating RNA polymerases. In bacteria, the transcription-repair coupling factor (TRCF; also known as Mfd) SF2 ATPase recognizes RNA polymerase stalled at a site of DNA damage, removes the enzyme from the DNA, and recruits the Uvr(A)BC nucleotide excision repair machinery via UvrA binding. Previous studies of TRCF revealed a molecular architecture incompatible with UvrA binding, leaving its recruitment mechanism unclear. Here, we examine the UvrA recognition determinants of TRCF using X-ray crystallography of a core TRCF-UvrA complex and probe the conformational flexibility of TRCF in the absence and presence of nucleotides using small-angle X-ray scattering. We demonstrate that the C-terminal domain of TRCF is inhibitory for UvrA binding, but not RNA polymerase release, and show that nucleotide binding induces concerted multidomain motions. Our studies suggest that autoinhibition of UvrA binding in TRCF may be relieved only upon engaging the DNA damage.

PubMed: 22331906
DOI: 10.1073/pnas.1115105109

実験手法

X-RAY DIFFRACTION (2.803 Å)