NMR assignment and backbone dynamics of the pore-forming domain of colicin A.
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.
Ibañez de Opakua
Alain
A
Unidad de Biofísica, CSIC-UPV/EHU, B masculine Sarriena, 48940 Leioa-Vizcaya, Spain.
Diercks
Tammo
T
Viguera
Ana R
AR
Blanco
Francisco J
FJ
D003087:Colicins / Q000737:chemistry*; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry; D009038:Motion; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012996:Solutions / Q000737:chemistry
D003087:Colicins; D029968:Escherichia coli Proteins; D009587:Nitrogen Isotopes; D012996:Solutions; D006859:Hydrogen