1FS0

COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI

1FS0 の概要

• エントリーDOI: 10.2210/pdb1fs0/pdb
• 関連するPDBエントリー: 1D8S
• 分子名称: ATP SYNTHASE EPSILON SUBUNIT, ATP SYNTHASE GAMMA SUBUNIT (3 entities in total)
• 機能のキーワード: atp synthase, coiled coil, gamma, epsilon, hydrolase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40639.79

構造登録者

Wilce, M.C.J.,Rodgers, A.J.W. (登録日: 2000-09-07, 公開日: 2001-05-01, 最終更新日: 2024-02-07)

主引用文献

Rodgers, A.J.,Wilce, M.C.
Structure of the gamma-epsilon complex of ATP synthase.
Nat.Struct.Biol., 7:1051-1054, 2000

PubMed Abstract: ATP synthases (F(1)F(o)-ATPases) use energy released by the movement of protons down a transmembrane electrochemical gradient to drive the synthesis of ATP, the universal biological energy currency. Proton flow through F(o) drives rotation of a ring of c-subunits and a complex of the gamma and epsilon-subunits, causing cyclical conformational changes in F(1) that are required for catalysis. The crystal structure of a large portion of F(1) has been resolved. However, the structure of the central portion of the enzyme, through which conformational changes in F(o) are communicated to F(1), has until now remained elusive. Here we report the crystal structure of a complex of the epsilon-subunit and the central domain of the gamma-subunit refined at 2.1 A resolution. The structure reveals how rotation of these subunits causes large conformational changes in F(1), and thereby provides new insights into energy coupling between F(o) and F(1).

PubMed: 11062562
DOI: 10.1038/80975

実験手法

X-RAY DIFFRACTION (2.1 Å)