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 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.
Gayen
Shovanlal
S
School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Nanyang 637551, Singapore.
Balakrishna
Asha M
AM
Grüber
Gerhard
G
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D019605:Euryarchaeota / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000648:ultrastructure*
D019843:Archaeal Proteins; D021122:Protein Subunits; C113203:A1A0 ATPase, Methanosarcina mazei; D006180:Proton-Translocating ATPases