Backbone 1H, 15N and 13C assignments for the subunit a of the E. coli ATP synthase

J Biomol NMR. 2004 Jul;29(3):439-40. doi: 10.1023/B:JNMR.0000032519.14221.20.

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.

Publication types

  • Letter

MeSH terms

  • 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

Substances

  • Carbon Isotopes
  • Escherichia coli Proteins
  • Nitrogen Isotopes
  • Protons
  • Water
  • Chloroform
  • Hydrogen
  • Bacterial Proton-Translocating ATPases
  • atpB protein, E coli
  • Methanol