3V4R

Crystal structure of a UvrB dimer-DNA complex

3V4R の概要

• エントリーDOI: 10.2210/pdb3v4r/pdb
• 分子名称: UvrABC system protein B, DNA: 5 -TACTGTTT-3, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: helicase motifs and a beta-hairpin, dna helicase, uvra, atp hydrolysis, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Bacillus subtilis; 詳細
• 細胞内の位置: Cytoplasm (By similarity): P37954
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 160207.64

構造登録者

Webster, M.P.J.,Jukes, R.,Barrett, T. (登録日: 2011-12-15, 公開日: 2012-07-04, 最終更新日: 2023-09-13)

主引用文献

Webster, M.P.,Jukes, R.,Zamfir, V.S.,Kay, C.W.,Bagneris, C.,Barrett, T.
Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexes.
Nucleic Acids Res., 40:8743-8758, 2012

PubMed Abstract: UvrB has a central role in the highly conserved UvrABC pathway functioning not only as a damage recognition element but also as an essential component of the lesion tracking machinery. While it has been recently confirmed that the tracking assembly comprises a UvrA2B2 heterotetramer, the configurations of the damage engagement and UvrB-DNA handover complexes remain obscure. Here, we present the first crystal structure of a UvrB dimer whose biological significance has been verified using both chemical cross-linking and electron paramagnetic resonance spectroscopy. We demonstrate that this dimeric species stably associates with UvrA and forms a UvrA2B2-DNA complex. Our studies also illustrate how signals are transduced between the ATP and DNA binding sites to generate the helicase activity pivotal to handover and formation of the UvrB2-DNA complex, providing key insights into the configurations of these important repair intermediates.

PubMed: 22753105
DOI: 10.1093/nar/gks633

実験手法

X-RAY DIFFRACTION (3.25 Å)