NMR assignment and backbone dynamics of the pore-forming domain of colicin A

Biomol NMR Assign. 2010 Apr;4(1):33-6. doi: 10.1007/s12104-009-9202-4. Epub 2009 Nov 26.

Abstract

Colicin A protein kills cells by opening voltage-dependent ion channels in the cytoplasmic membrane. The C-terminal domain of colicin A retains the full protein's ability to form membrane pores, making it an excellent model for in vitro studies of protein-membrane interaction. We report here the NMR assignment and backbone dynamics of this domain in solution. The chemical shifts identify ten alpha-helices that match those observed in the crystal structure, while the (15)N{(1)H} NOEs show differential fast mobility for some of the inter-helical loops and the chain ends. This analysis provides the basis for further NMR studies of this channel forming protein and its interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Colicins / chemistry*
  • Escherichia coli
  • Escherichia coli Proteins / chemistry*
  • Hydrogen / chemistry
  • Motion
  • Nitrogen Isotopes / chemistry
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Solutions / chemistry

Substances

  • Colicins
  • Escherichia coli Proteins
  • Nitrogen Isotopes
  • Solutions
  • Hydrogen