2IS1

Crystal structure of UvrD-DNA-SO4 complex

2IS1 の概要

• エントリーDOI: 10.2210/pdb2is1/pdb
• 分子名称: 5'-D(*GP*CP*AP*GP*TP*GP*CP*TP*CP*GP*TP*TP*TP*TP*TP*TP*T)-3', 5'-D(*CP*GP*AP*GP*CP*AP*CP*TP*GP*C)-3', DNA helicase II, ... (7 entities in total)
• 機能のキーワード: dna helicase, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 173510.18

構造登録者

Yang, W.,Lee, J.Y. (登録日: 2006-10-16, 公開日: 2007-01-09, 最終更新日: 2023-08-30)

主引用文献

Lee, J.Y.,Yang, W.
UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke.
Cell(Cambridge,Mass.), 127:1349-1360, 2006

PubMed Abstract: Helicases use the energy derived from nucleoside triphosphate hydrolysis to unwind double helices in essentially every metabolic pathway involving nucleic acids. Earlier crystal structures have suggested that DNA helicases translocate along a single-stranded DNA in an inchworm fashion. We report here a series of crystal structures of the UvrD helicase complexed with DNA and ATP hydrolysis intermediates. These structures reveal that ATP binding alone leads to unwinding of 1 base pair by directional rotation and translation of the DNA duplex, and ADP and Pi release leads to translocation of the developing single strand. Thus DNA unwinding is achieved by a two-part power stroke in a combined wrench-and-inchworm mechanism. The rotational angle and translational distance of DNA define the unwinding step to be 1 base pair per ATP hydrolyzed. Finally, a gateway for ssDNA translocation and an alternative strand-displacement mode may explain the varying step sizes reported previously.

PubMed: 17190599
DOI: 10.1016/j.cell.2006.10.049

実験手法

X-RAY DIFFRACTION (2.9 Å)