4DFC

Core UvrA/TRCF complex

Summary for 4DFC

• Entry DOI: 10.2210/pdb4dfc/pdb
• Descriptor: Transcription-repair-coupling factor, UvrABC system protein A (2 entities in total)
• Functional Keywords: alpha/beta domains, dna repair, atp binding, dna binding, nucleotide excision repair, hydrolase-dna binding protein complex, hydrolase/dna binding protein
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm (By similarity): P0A698
• Total number of polymer chains: 4
• Total formula weight: 49083.57

Authors

Deaconescu, A.M.,Grigorieff, N. (deposition date: 2012-01-23, release date: 2012-05-02, Last modification date: 2023-09-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.803 Å)