1N03

Model for Active RecA Filament

1N03 の概要

• エントリーDOI: 10.2210/pdb1n03/pdb
• 分子名称: RecA protein, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: helical polymer, dna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 268186.01

構造登録者

VanLoock, M.S.,Yu, X.,Yang, S.,Lai, A.L.,Low, C.,Campbell, M.J.,Egelman, E.H. (登録日: 2002-10-10, 公開日: 2003-02-25, 最終更新日: 2024-02-14)

主引用文献

VanLoock, M.S.,Yu, X.,Yang, S.,Lai, A.L.,Low, C.,Campbell, M.J.,Egelman, E.H.
ATP-Mediated Conformational Changes in the RecA Filament
Structure, 11:187-196, 2003

PubMed Abstract: The crystal structure of the E. coli RecA protein was solved more than 10 years ago, but it has provided limited insight into the mechanism of homologous genetic recombination. Using electron microscopy, we have reconstructed five different states of RecA-DNA filaments. The C-terminal lobe of the RecA protein is modulated by the state of the distantly bound nucleotide, and this allosteric coupling can explain how mutations and truncations of this C-terminal lobe enhance RecA's activity. A model generated from these reconstructions shows that the nucleotide binding core is substantially rotated from its position in the RecA crystal filament, resulting in ATP binding between subunits. This simple rotation can explain the large cooperativity in ATP hydrolysis observed for RecA-DNA filaments.

PubMed: 12575938
DOI: 10.1016/S0969-2126(03)00003-0

実験手法

ELECTRON MICROSCOPY (20 Å)