2EYQ

Crystal structure of Escherichia coli transcription-repair coupling factor

Summary for 2EYQ

• Entry DOI: 10.2210/pdb2eyq/pdb
• Descriptor: Transcription-repair coupling factor, SULFATE ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: mfd, sf2 atpase, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 262369.23

Authors

Deaconescu, A.M.,Darst, S.A. (deposition date: 2005-11-09, release date: 2006-02-28, Last modification date: 2024-02-14)

Primary citation

Deaconescu, A.M.,Chambers, A.L.,Smith, A.J.,Nickels, B.E.,Hochschild, A.,Savery, N.J.,Darst, S.A.
Structural basis for bacterial transcription-coupled DNA repair.
Cell(Cambridge,Mass.), 124:507-520, 2006

PubMed Abstract: Coupling of transcription and DNA repair in bacteria is mediated by transcription-repair coupling factor (TRCF, the product of the mfd gene), which removes transcription elongation complexes stalled at DNA lesions and recruits the nucleotide excision repair machinery to the site. Here we describe the 3.2 A-resolution X-ray crystal structure of Escherichia coli TRCF. The structure consists of a compact arrangement of eight domains, including a translocation module similar to the SF2 ATPase RecG, and a region of structural similarity to UvrB. Biochemical and genetic experiments establish that another domain with structural similarity to the Tudor-like domain of the transcription elongation factor NusG plays a critical role in TRCF/RNA polymerase interactions. Comparison with the translocation module of RecG as well as other structural features indicate that TRCF function involves large-scale conformational changes. These data, along with a structural model for the interaction of TRCF with the transcription elongation complex, provide mechanistic insights into TRCF function.

PubMed: 16469698
DOI: 10.1016/j.cell.2005.11.045

Experimental method

X-RAY DIFFRACTION (3.2 Å)