PMID:9466900

Citation	Bainbridge, G, Mobasheri, H, Armstrong, GA, Lea, EJ and Lakey, JH (1998) Voltage-gating of Escherichia coli porin: a cystine-scanning mutagenesis study of loop 3. J. Mol. Biol. 275:171-6
Abstract	Porins, such as Escherichia coli OmpF, provide the only reported example of a voltage-gated channel where the three-dimensional structure is known to high resolution. Mutations that affect voltage-gating are clustered around the eyelet region, which is a mid-channel constriction caused by a polypeptide loop (L3) folding inside the lumen of this beta-barrel pore. These data, combined with molecular dynamics simulations, indicate that voltage-gating may involve L3 displacement. We have constructed six double cysteine OmpF mutants, five of which form disulphide bonds fixing L3 in the conformation determined by X-ray crystallography. These channels have altered single-channel conductances but unimpaired voltage-gating. The data show that L3 movement is not required for voltage-gating.
Links	PubMed Online version:10.1006/jmbi.1997.1474
Keywords	Amino Acid Sequence; Amino Acid Substitution; Cystine; Disulfides; Escherichia coli/physiology; Ion Channel Gating; Lipid Bilayers; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Porins/chemistry; Porins/metabolism; Protein Conformation; Recombinant Proteins/chemistry
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