Interaction of the Thermoplasma acidophilum A₁A₀-ATP synthase peripheral stalk with the catalytic domain

Abstract 

The peripheral stalk of the archaeal ATP synthase (A₁A₀)-ATP synthase is formed by the heterodimeric EH complex and is part of the stator domain, which counteracts the torque of rotational catalysis. Here we used nuclear magnetic resonance spectroscopy to probe the interaction of the C-terminal domain of the EH heterodimer (E_CT1H_CT) with the N-terminal 23 residues of the B subunit (B_NT). The data show a specific interaction of B_NT peptide with 26 residues of the E_CT1H_CT domain, thereby providing a molecular picture of how the peripheral stalk is anchored to the A₃B₃ catalytic domain in A₁A₀.

Structured summary

MINT-7260681: Hct (refseq:NP_393485), Ect1 (uniprotkb:Q9HM68) and Bnt (uniprotkb:Q9HM64) physically interact (MI:0915) by nuclear magnetic resonance (MI:0077)

Abbreviations: A₁A₀, archaeal ATP synthase, A₁, water soluble domain of the A₁A₀-ATP synthase, A₀, membrane bound domain of the A₁A₀-ATP synthase, NMR, nuclear magnetic resonance, CSI, chemical shift index, HSQC, heteroatom single quantum coherence, ppm, parts per million

Keywords: Archaeal ATP synthase, Molecular rotary motor, Peripheral stalk, Protein structure, Nuclear magnetic resonance spectroscopy