2KK7

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

(2009) J Bioenerg Biomembr 41: 343-348

• PubMed: 19760172 Search on PubMed
• DOI: https://doi.org/10.1007/s10863-009-9237-3
• Primary Citation of Related Structures:  
  2KK7


• PubMed Abstract: 
  

  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.

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Organizational Affiliation: 

School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Nanyang 637551, Singapore.