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Eur J Biochem. 1999 Apr;261(2):459-67.

NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles.

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1
Mikrobiologisches Institut, Eidgenössische Technische Hochschule, Zürich, Switzerland.

Abstract

The structure of the Na+, Li+ or H+-binding c subunit of the ATP synthase from Propionigenium modestum was studied by NMR. Subunit c in dodecylsulphate micelles consists of four alpha-helical segments, I-IV, that are connected by short linker peptides with non-regular secondary structures. We propose that helices I (V4-I26) and IV (I69-V85) are membrane-spanning structures, and that helices II and III and the intervening hydrophilic loop are located in the cytoplasm. The Na+-binding residues Q32, E65 and S66 are located in the I-->II and III-->IV helix connections, probably near the membrane surface on the cytoplasmic side.

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