Altered voltage sensitivity of mutant OmpC porin channels

FEBS Letters
N D BishopS Spiro

Abstract

Single OmpC porin channels have been reconstituted in planar bilayer membranes. Wild-type OmpC forms trimers which are largely insensitive to voltages below 250 mV.A single-point mutation of the ompC gene has been prepared resulting in replacement of Trp56 by Cys in the eyelet region of the channel wall in a highly conserved segment of the polypeptide. The monomeric channels of which the trimer is composed have smaller conductivity in 1 M NaCl (400 +/- 20 pS, mean and S.E.M., n=30) and increased voltage sensitivity by comparison with the wild-type under similar conditions, whereas other (Dex) mutants form larger channels and display different behaviour. Further, by treatment in SDS solutions at different temperatures, the W56C mutant has been shown to be less stable than either the wild-type or the Dex mutants.

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Citations

Jul 31, 1998·Protein Science : a Publication of the Protein Society·B SchmidG E Schulz
Dec 20, 2011·Journal of the American Chemical Society·Christopher D SpicerBenjamin G Davis
Oct 25, 2008·Molecular Membrane Biology·Brian LaumanAnne H Delcour
Nov 18, 2008·Chembiochem : a European Journal of Chemical Biology·Min ChenHagan Bayley
May 23, 2006·Archives of Biochemistry and Biophysics·Conceição A S A Minetti, David P Remeta
Jun 2, 2020·Journal of Chemical Information and Modeling·Jigneshkumar Dahyabhai PrajapatiUlrich Kleinekathöfer
Dec 23, 2008·Biochimica Et Biophysica Acta·Anne H Delcour

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