3ZO6

Crystal structure of Bacillus pseudofirmus OF4 mutant ATP synthase c12 ring.

3ZO6 の概要

• エントリーDOI: 10.2210/pdb3zo6/pdb
• 分子名称: ATP synthase subunit c (1 entity in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Bacillus pseudofirmus OF4
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 83512.91

構造登録者

Preiss, L.,Yildiz, O.,Meier, T. (登録日: 2013-02-20, 公開日: 2013-05-01, 最終更新日: 2024-10-09)

主引用文献

Preiss, L.,Klyszejko, A.L.,Hicks, D.B.,Liu, J.,Fackelmayer, O.J.,Yildiz, O.,Krulwich, T.A.,Meier, T.
The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacillus pseudofirmus OF4.
Proc. Natl. Acad. Sci. U.S.A., 110:7874-7879, 2013

PubMed Abstract: The c-rings of ATP synthases consist of individual c-subunits, all of which harbor a conserved motif of repetitive glycine residues (GxGxGxG) important for tight transmembrane α-helix packing. The c-ring stoichiometry determines the number of ions transferred during enzyme operation and has a direct impact on the ion-to-ATP ratio, a cornerstone parameter of cell bioenergetics. In the extreme alkaliphile Bacillus pseudofirmus OF4, the glycine motif is replaced by AxAxAxA. We performed a structural study on two mutants with alanine-to-glycine changes using atomic force microscopy and X-ray crystallography, and found that mutants form smaller c12 rings compared with the WT c13. The molar growth yields of B. pseudofirmus OF4 cells on malate further revealed that the c12 mutants have a considerably reduced capacity to grow on limiting malate at high pH. Our results demonstrate that the mutant ATP synthases with either c12 or c13 can support ATP synthesis, and also underscore the critical importance of an alanine motif with c13 ring stoichiometry for optimal growth at pH >10. The data indicate a direct connection between the precisely adapted ATP synthase c-ring stoichiometry and its ion-to-ATP ratio on cell physiology, and also demonstrate the bioenergetic challenges and evolutionary adaptation strategies of extremophiles.

PubMed: 23613590
DOI: 10.1073/pnas.1303333110

実験手法

X-RAY DIFFRACTION (4.104 Å)