NMR solution structure of the N-terminal domain of subunit E (E1–52) of A1AO ATP synthase from Methanocaldococcus jannaschii

The N-termini of E and H of A1AO ATP synthase have been shown to interact and an NMR structure of N-terminal H1–47 has been solved recently. In order to understand the E-H assembly and the N-terminal structure of E, the truncated construct E1–52 of Methanocaldococcus jannaschii A1AO ATP synthase was produced, purified and the solution structure of E1–52 was determined by NMR spectroscopy. The protein is 60.5 Å in length and forms an α helix between the residues 8–48. The molecule is amphipathic with a strip of hydrophobic residues, discussed as a possible helix-helix interaction with neighboring subunit H.