Download MendeleyCrystal structure of a colicin N fragment suggests a model for toxicity.
Vetter, I.R., Parker, M.W., Tucker, A.D., Lakey, J.H., Pattus, F., Tsernoglou, D.(1998) Structure 6: 863-874
- PubMed: 9687368
- DOI: https://doi.org/10.1016/s0969-2126(98)00088-4
- Primary Citation of Related Structures:
1A87 - PubMed Abstract:
Pore-forming colicins are water-soluble bacteriocins capable of binding to and translocating through the Escherichia coli cell envelope. They then undergo a transition to a transmembrane ion channel in the cytoplasmic membrane leading to bacterial death. Colicin N is the smallest pore-forming colicin known to date (40 kDa instead of the more usual 60 kDa) and the crystal structure of its membrane receptor, the porin OmpF, is already known. Structural knowledge of colicin N is therefore important for a molecular understanding of colicin toxicity and is relevant to toxic mechanisms in general.
Organizational Affiliation:
European Molecular Biology Laboratory, Heidelberg, Germany. ingrid.vetter@mpi-dortmund.mpg.de
