2G88

MSRECA-dATP COMPLEX

2G88 の概要

• エントリーDOI: 10.2210/pdb2g88/pdb
• 関連するPDBエントリー: 1ubc
• 分子名称: Protein recA, MAGNESIUM ION, 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: recombination, dna-repair
• 由来する生物種: Mycobacterium smegmatis
• 細胞内の位置: Cytoplasm (By similarity): Q59560
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38543.28

構造登録者

Krishna, R.,Manjunath, G.P.,Kumar, P.,Surolia, A.,Chandra, N.R.,Muniyappa, K.,Vijayan, M. (登録日: 2006-03-02, 公開日: 2006-05-16, 最終更新日: 2023-08-30)

主引用文献

Krishna, R.,Manjunath, G.P.,Kumar, P.,Surolia, A.,Chandra, N.R.,Muniyappa, K.,Vijayan, M.
Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery.
Nucleic Acids Res., 34:2186-2195, 2006

PubMed Abstract: RecA protein is a crucial and central component of the homologous recombination and DNA repair machinery. Despite numerous studies on the protein, several issues concerning its action, including the allosteric regulation mechanism have remained unclear. Here we report, for the first time, a crystal structure of a complex of Mycobacterium smegmatis RecA (MsRecA) with dATP, which exhibits a fully ordered C-terminal domain, with a second dATP molecule bound to it. ATP binding is an essential step for all activities of RecA, since it triggers the formation of active nucleoprotein filaments. In the crystal filament, dATP at the first site communicates with a dATP of the second site of an adjacent subunit, through conserved residues, suggesting a new route for allosteric regulation. In addition, subtle but definite changes observed in the orientation of the nucleotide at the first site and in the positions of the segment preceding loop L2 as well as in the segment 102-105 situated between the 2 nt, all appear to be concerted and suggestive of a biological role for the second bound nucleotide.

PubMed: 16648362
DOI: 10.1093/nar/gkl107

実験手法

X-RAY DIFFRACTION (3.2 Å)