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

J Bioenerg Biomembr. 2009 Aug;41(4):343-8. doi: 10.1007/s10863-009-9237-3.


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 A in length and forms an alpha 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / ultrastructure*
  • Euryarchaeota / enzymology*
  • Magnetic Resonance Spectroscopy / methods*
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Tertiary
  • Protein Subunits
  • Proton-Translocating ATPases / chemistry*
  • Proton-Translocating ATPases / ultrastructure*


  • Archaeal Proteins
  • Protein Subunits
  • A1A0 ATPase, Methanosarcina mazei
  • Proton-Translocating ATPases

Associated data

  • PDB/2KK7