3V6I

Crystal structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase at 2.25 A resolution

3V6I の概要

• エントリーDOI: 10.2210/pdb3v6i/pdb
• 関連するPDBエントリー: 3K5B
• 分子名称: V-type ATP synthase subunit E, V-type ATP synthase, subunit (VAPC-THERM), CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: peripheral stator stalk, right handed coiled-coil, atpase/synthase, atp binding, membrane, 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: 64803.24

構造登録者

Stewart, A.G.,Lee, L.K.,Donohoe, M.,Chaston, J.J.,Stock, D. (登録日: 2011-12-19, 公開日: 2012-02-22, 最終更新日: 2024-03-20)

主引用文献

Stewart, A.G.,Lee, L.K.,Donohoe, M.,Chaston, J.J.,Stock, D.
The dynamic stator stalk of rotary ATPases
Nat Commun, 3:687-687, 2012

PubMed Abstract: Rotary ATPases couple ATP hydrolysis/synthesis with proton translocation across biological membranes and so are central components of the biological energy conversion machinery. Their peripheral stalks are essential components that counteract torque generated by rotation of the central stalk during ATP synthesis or hydrolysis. Here we present a 2.25-Å resolution crystal structure of the peripheral stalk from Thermus thermophilus A-type ATPase/synthase. We identify bending and twisting motions inherent within the structure that accommodate and complement a radial wobbling of the ATPase headgroup as it progresses through its catalytic cycles, while still retaining azimuthal stiffness necessary to counteract rotation of the central stalk. The conformational freedom of the peripheral stalk is dictated by its unusual right-handed coiled-coil architecture, which is in principle conserved across all rotary ATPases. In context of the intact enzyme, the dynamics of the peripheral stalks provides a potential mechanism for cooperativity between distant parts of rotary ATPases.

PubMed: 22353718
DOI: 10.1038/ncomms1693

実験手法

X-RAY DIFFRACTION (2.25 Å)