Backbone 1H, 15N and 13C assignments for the subunit a of the E. coli ATP synthase.
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.
Dmitriev
Oleg Y
OY
Abildgaard
Frits
F
Markley
John L
JL
Fillingame
Robert H
RH
D000595:Amino Acid Sequence; D025243:Bacterial Proton-Translocating ATPases / Q000737:chemistry*; D002247:Carbon Isotopes; D002462:Cell Membrane / Q000378:metabolism; D002725:Chloroform / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D000432:Methanol / Q000737:chemistry; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011522:Protons; D014867:Water / Q000737:chemistry
D002247:Carbon Isotopes; D029968:Escherichia coli Proteins; D009587:Nitrogen Isotopes; D011522:Protons; D014867:Water; D002725:Chloroform; D006859:Hydrogen; D025243:Bacterial Proton-Translocating ATPases; C074428:atpB protein, E coli; D000432:Methanol