2X2V

Structural basis of a novel proton-coordination type in an F1Fo-ATP synthase rotor ring

2X2V の概要

• エントリーDOI: 10.2210/pdb2x2v/pdb
• 分子名称: ATP SYNTHASE SUBUNIT C, dodecyl 2-(trimethylammonio)ethyl phosphate, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: membrane protein, ion transport, atp synthesis, transmembrane, cf(0), membrane, transport, c-ring rotor, hydronium ion, ion binding pocket, hydrogen ion transport
• 由来する生物種: BACILLUS PSEUDOFIRMUS OF4
• 細胞内の位置: Cell membrane; Multi-pass membrane protein (Potential): P22483
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 95635.90

構造登録者

Preiss, L.,Yildiz, O.,Hicks, D.B.,Krulwich, T.A.,Meier, T. (登録日: 2010-01-18, 公開日: 2010-08-18, 最終更新日: 2024-11-20)

主引用文献

Preiss, L.,Yildiz, O.,Hicks, D.B.,Krulwich, T.A.,Meier, T.
A New Type of Proton Coordination in an F(1)F(O)- ATP Synthase Rotor Ring.
Plos Biol., 8:443-, 2010

PubMed Abstract: We solved the crystal structure of a novel type of c-ring isolated from Bacillus pseudofirmus OF4 at 2.5 A, revealing a cylinder with a tridecameric stoichiometry, a central pore, and an overall shape that is distinct from those reported thus far. Within the groove of two neighboring c-subunits, the conserved glutamate of the outer helix shares the proton with a bound water molecule which itself is coordinated by three other amino acids of outer helices. Although none of the inner helices contributes to ion binding and the glutamate has no other hydrogen bonding partner than the water oxygen, the site remains in a stable, ion-locked conformation that represents the functional state present at the c-ring/membrane interface during rotation. This structure reveals a new, third type of ion coordination in ATP synthases. It appears in the ion binding site of an alkaliphile in which it represents a finely tuned adaptation of the proton affinity during the reaction cycle.

PubMed: 20689804
DOI: 10.1371/JOURNAL.PBIO.1000443

実験手法

X-RAY DIFFRACTION (2.5 Å)