Interaction of the Thermoplasma acidophilum A1A0-ATP synthase peripheral stalk with the catalytic domain |
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| Authors: | Erik Kish-Trier |
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| Affiliation: | Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA |
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| 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 (ECT1HCT) with the N-terminal 23 residues of the B subunit (BNT). The data show a specific interaction of BNT peptide with 26 residues of the ECT1HCT domain, thereby providing a molecular picture of how the peripheral stalk is anchored to the A3B3 catalytic domain in A1A0.Structured summaryMINT-7260681: Hct (refseq:NP_393485), Ect1 (uniprotkb:Q9HM68) and Bnt (uniprotkb:Q9HM64) physically interact (MI:0915) by nuclear magnetic resonance (MI:0077) |
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| Keywords: | 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 |
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