3K5B

Crystal structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase

3K5B の概要

• エントリーDOI: 10.2210/pdb3k5b/pdb
• 分子名称: V-type ATP synthase, subunit (VAPC-THERM), V-type ATP synthase subunit E (2 entities in total)
• 機能のキーワード: right handed coiled coil, vacuolar atpase/synthase, v-type atpase/synthase, a-type atpase/synthase, peripheral stator, peripheral stalk, atp synthesis, hydrogen ion transport, ion transport, transport, hydrolase
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 65111.04

構造登録者

Lee, L.K.,Stewart, A.G.,Donohoe, M.,Bernal, R.A.,Stock, D. (登録日: 2009-10-07, 公開日: 2010-02-23, 最終更新日: 2024-10-09)

主引用文献

Lee, L.K.,Stewart, A.G.,Donohoe, M.,Bernal, R.A.,Stock, D.
The structure of the peripheral stalk of Thermus thermophilus H(+)-ATPase/synthase.
Nat.Struct.Mol.Biol., 17:373-378, 2010

PubMed Abstract: Proton-translocating ATPases are ubiquitous protein complexes that couple ATP catalysis with proton translocation via a rotary catalytic mechanism. The peripheral stalks are essential components that counteract torque generated from proton translocation during ATP synthesis or from ATP hydrolysis during proton pumping. Despite their essential role, the peripheral stalks are the least conserved component of the complexes, differing substantially between subtypes in composition and stoichiometry. We have determined the crystal structure of the peripheral stalk of the A-type ATPase/synthase from Thermus thermophilus consisting of subunits E and G. The structure contains a heterodimeric right-handed coiled coil, a protein fold never observed before. We have fitted this structure into the 23 A resolution EM density of the intact A-ATPase complex, revealing the precise location of the peripheral stalk and new implications for the function and assembly of proton-translocating ATPases.

PubMed: 20173764
DOI: 10.1038/nsmb.1761

実験手法

X-RAY DIFFRACTION (3.1 Å)