Characterisation of a mobile protein-binding epitope in the translocation domain of colicin E9

The 61 kDa colicin E9 protein toxin enters the cytoplasm of susceptible cells by interacting with outer membrane and periplasmic helper proteins, and kills them by hydrolysing their DNA. The membrane translocation function is located in the N-terminal domain of the colicin, with a key signal sequenc...

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Veröffentlicht in:	Journal of biomolecular NMR 2004-09, Vol.30 (1), p.81-96
Hauptverfasser:	Macdonald, Colin J, Tozawa, Kaeko, Collins, Emily S, Penfold, Christopher N, James, Richard, Kleanthous, Colin, Clayden, Nigel J, Moore, Geoffrey R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino acids Binding Sites Biological Transport, Active Carbon Isotopes Colicins - chemistry Colicins - genetics Colicins - metabolism Deoxyribonucleases - metabolism Epitopes - metabolism Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Molecular Weight Nitrogen Isotopes Nuclear Magnetic Resonance, Biomolecular Polymers Protein Binding Protein Conformation Protein Structure, Tertiary Proteins Quantum Theory Residues Toxins Translocation
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