title: Pore-forming colicins and their relatives.
abstract: The pore-forming colicins, the first proteins that were capable of forming voltage-dependent ion channels to be sequenced, have turned out to be both less tractable and more mysterious than imagined; yet they have proved interesting at every step of their short journey from producing cell to vanquished target cell. Starting out as a remarkably extended water-soluble protein, the colicin molecule is designed to interact simultaneously with several components of the complex membrane of the target cell, transform itself into a membrane protein, and become an ion channel with inscrutable properties. Unraveling how it does all this appears to be leading us into the dark recesses of protein/protein and protein/membrane interaction, where lurk fundamental processes reluctantly waiting to be revealed.
authors: School of Biochemistry and Genetics, Medical School, University of Newcastle, NE2 4HH, UK.
authors: J H
authors: JH
authors: Lakey
authors: S L
authors: SL
authors: Slatin
mesh_terms: D000818:Animals; D001435:Bacteriophages / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism; D002463:Cell Membrane Permeability; D003087:Colicins / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins; D005656:Fungal Proteins / Q000737:chemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007425:Intracellular Membranes / Q000737:chemistry; D007473:Ion Channels / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism
chemical_list: D003087:Colicins; D029968:Escherichia coli Proteins; D005656:Fungal Proteins; D007473:Ion Channels; D011956:Receptors, Cell Surface; C117550:TOL protein, Neurospora crassa; C028593:colicin receptor, E coli