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Article

Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase.

The Journal of biological chemistry - 28 May 1999

Dmitriev O, Jones P C, Jiang W, Fillingame R H

Abstract excerpt

The structure of the N-terminal transmembrane domain (residues 1-34) of subunit b of the Escherichia coli F0F1-ATP synthase has been solved by two-dimensional 1H NMR in a membrane mimetic solvent mixture of chloroform/methanol/H2O (4:4:1). Residues 4-22 form an alpha-helix, which is likely to span the hydrophobic domain of the lipid bilayer to anchor the largely hydrophilic subunit b in the membrane. The helical...

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Identifiers

PMID: 10336456
DOI: 10.1074/jbc.274.22.15598

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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