2EYQ

Crystal structure of Escherichia coli transcription-repair coupling factor

2EYQ の概要

• エントリーDOI: 10.2210/pdb2eyq/pdb
• 分子名称: Transcription-repair coupling factor, SULFATE ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: mfd, sf2 atpase, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 262369.23

構造登録者

Deaconescu, A.M.,Darst, S.A. (登録日: 2005-11-09, 公開日: 2006-02-28, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.2 Å)