PMID:15213458

Citation	Dmitriev, OY, Abildgaard, F, Markley, JL and Fillingame, RH (2004) Backbone 1H, 15N and 13C assignments for the subunit a of the E. coli ATP synthase. J. Biomol. NMR 29:439-40
Abstract	The structure of the 30 KDa subunit a of the membrane component (F(0)) of E. coli ATP synthase is investigated in a mixture of chloroform, methanol and water, a solvent previously used for solving the structure of another integral membrane protein, subunit c. Near complete backbone chemical shift assignments were made from a set of TROSY experiments including HNCO, HNCA, HN(CA)CB, HN(CO)CACB and 4D HNCOCA and HNCACO. Secondary structure of subunit a was predicted from the backbone chemical shifts using TALOS program. The protein was found to consist of multiple elongated alpha-helical segments. This finding is generally consistent with previous predictions of multiple transmembrane alpha-helices in this polytopic protein.
Links	PubMed Online version:10.1023/B:JNMR.0000032519.14221.20
Keywords	Amino Acid Sequence; Bacterial Proton-Translocating ATPases/chemistry; Carbon Isotopes; Cell Membrane/metabolism; Chloroform/chemistry; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Hydrogen; Magnetic Resonance Spectroscopy/methods; Methanol/chemistry; Molecular Sequence Data; Nitrogen Isotopes; Protein Structure, Secondary; Protein Structure, Tertiary; Protons; Water/chemistry
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