2E5U

C-terminal domain of Epsilon subunit of F1F0-ATP synthase from the Thermophilic Bacillus PS3

2E5U の概要

• エントリーDOI: 10.2210/pdb2e5u/pdb
• 関連するPDBエントリー: 1AQT 1BSN 2E5T 2E5Y
• 分子名称: ATP synthase epsilon chain (1 entity in total)
• 機能のキーワード: atp synthase, f1fo atp synthase, f1-atpase, epsilon subunit, atp, hydrolase
• 由来する生物種: Bacillus sp. PS3
• 細胞内の位置: Cell membrane; Peripheral membrane protein (By similarity): P07678
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4735.50

構造登録者

Yagi, H.,Akutsu, H. (登録日: 2006-12-25, 公開日: 2007-07-10, 最終更新日: 2024-05-29)

主引用文献

Yagi, H.,Kajiwara, N.,Tanaka, H.,Tsukihara, T.,Kato-Yamada, Y.,Yoshida, M.,Akutsu, H.
Structures of the thermophilic F1-ATPase {varepsilon} subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1
Proc.Natl.Acad.Sci.Usa, 104:11233-11238, 2007

PubMed Abstract: The epsilon subunit of bacterial and chloroplast F(o)F(1)-ATP synthases modulates their ATP hydrolysis activity. Here, we report the crystal structure of the ATP-bound epsilon subunit from a thermophilic Bacillus PS3 at 1.9-A resolution. The C-terminal two alpha-helices were folded into a hairpin, sitting on the beta sandwich structure, as reported for Escherichia coli. A previously undescribed ATP binding motif, I(L)DXXRA, recognizes ATP together with three arginine and one glutamate residues. The E. coli epsilon subunit binds ATP in a similar manner, as judged on NMR. We also determined solution structures of the C-terminal domain of the PS3 epsilon subunit and relaxation parameters of the whole molecule by NMR. The two helices fold into a hairpin in the presence of ATP but extend in the absence of ATP. The latter structure has more helical regions and is much more flexible than the former. These results suggest that the epsilon C-terminal domain can undergo an arm-like motion in response to an ATP concentration change and thereby contribute to regulation of F(o)F(1)-ATP synthase.

PubMed: 17581881
DOI: 10.1073/pnas.0701045104

実験手法

SOLUTION NMR