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Identification of aqueous access residues of the sodium half channel in transmembrane helix 5 of the F_o-a subunit of Propionigenium modestum ATP synthase.

ABSTRACT: The F_o-a subunit of the Na⁺-transporting F_oF₁ ATP synthase from Propionigenium modestum plays a key role in Na⁺ transport. It forms half channels that allow Na⁺ to enter and leave the buried carboxyl group on F_o-c subunits. The essential Arg residue R226, which faces the carboxyl group of F_o-c subunits in the middle of transmembrane helix 5 of the F_o-a subunit, separates the cytoplasmic side and periplasmic half-channels. To elucidate contributions of other amino acid residues of transmembrane helix 5 using hybrid F_oF₁ (F_o from P. modestum and F₁ from thermophilic Bacillus PS3), 25 residues were indiv

SUBMITTER: Mitome N

PROVIDER: S-EPMC5448315 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

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Dataset Information

Identification of aqueous access residues of the sodium half channel in transmembrane helix 5 of the F_o-a subunit of Propionigenium modestum ATP synthase.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dataset Information

Identification of aqueous access residues of the sodium half channel in transmembrane helix 5 of the Fo-a subunit of Propionigenium modestum ATP synthase.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Identification of aqueous access residues of the sodium half channel in transmembrane helix 5 of the F_o-a subunit of Propionigenium modestum ATP synthase.