4CBJ
The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology
4CBJ の概要
エントリーDOI | 10.2210/pdb4cbj/pdb |
関連するPDBエントリー | 4CBK |
分子名称 | ATP SYNTHASE SUBUNIT C, dodecyl 2-(trimethylammonio)ethyl phosphate, TRIS(HYDROXYETHYL)AMINOMETHANE, ... (6 entities in total) |
機能のキーワード | f1fo-atp synthase, c-ring rotor, ion binding pocket, transferase |
由来する生物種 | BACILLUS PSEUDOFIRMUS OF4 詳細 |
細胞内の位置 | Cell membrane; Multi-pass membrane protein (Potential): P22483 P22483 |
タンパク質・核酸の鎖数 | 13 |
化学式量合計 | 95899.72 |
構造登録者 | |
主引用文献 | Preiss, L.,Langer, J.D.,Hicks, D.B.,Liu, J.,Yildiz, O.,Krulwich, T.A.,Meier, T. The C-Ring Ion-Binding Site of the ATP Synthase from Bacillus Pseudofirmus of4 is Adapted to Alkaliphilic Lifestyle. Mol.Microbiol., 92:973-, 2014 Cited by PubMed Abstract: In the c-ring rotor of ATP synthases ions are shuttled across the membrane during ATP synthesis by a unique rotary mechanism. We investigated characteristics of the c-ring from the alkaliphile Bacillus pseudofirmus OF4 with respect to evolutionary adaptations to operate with protons at high environmental pH. The X-ray structures of the wild-type c13 ring at pH 9.0 and a 'neutralophile-like' mutant (P51A) at pH 4.4, at 2.4 and 2.8 Å resolution, respectively, reveal a dependency of the conformation and protonation state of the proton-binding glutamate (E(54) ) on environmental hydrophobicity. Faster labelling kinetics with the inhibitor dicyclohexylcarbodiimide (DCCD) demonstrate a greater flexibility of E(54) in the mutant due to reduced water occupancy within the H(+) binding site. A second 'neutralophile-like' mutant (V21N) shows reduced growth at high pH, which is explained by restricted conformational freedom of the mutant's E(54) carboxylate. The study directly connects subtle structural adaptations of the c-ring ion binding site to in vivo effects of alkaliphile cell physiology. PubMed: 24707994DOI: 10.1111/MMI.12605 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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