J Bioenerg Biomembr. 2009 Aug;41(4):343-8.

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

Source

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

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.

PMID:: 19760172; [PubMed - indexed for MEDLINE]

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Research Support, Non-U.S. Gov't

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Secondary Source ID

PDB/2KK7

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Structures reported by this article

Nmr Solution Structure Of The N Terminal Domain Of Subunit E (E1-52) Of A1ao Atp Synthase From Methanocaldococcus Jannaschii

PDB: 2KK7

Source: Methanocaldococcus jannaschii

Method: Solution Nmr

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