Structural highlights
Function
[VATE_METJA] Produces ATP from ADP in the presence of a proton gradient across the membrane (By similarity).
Publication Abstract from PubMed
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.
NMR solution structure of the N-terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii.,Gayen S, Balakrishna AM, Gruber G J Bioenerg Biomembr. 2009 Aug;41(4):343-8. PMID:19760172[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gayen S, Balakrishna AM, Gruber G. 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. PMID:19760172 doi:10.1007/s10863-009-9237-3
