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Voltage gating is a fundamental feature of porin and toxin β‐barrel membrane channels
Author(s) -
Bainbridge Graeme,
Gokce Isa,
Lakey Jeremy H
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00761-3
Subject(s) - porin , gating , barrel (horology) , bacterial outer membrane , biophysics , voltage dependent anion channel , chemistry , membrane , ion channel , mutant , lipid bilayer , crystallography , biochemistry , biology , materials science , escherichia coli , receptor , composite material , gene
Beta‐barrel pores are found in outer membrane porins of Gram‐negative bacteria, bacterial toxins and mitochondrial channels. Apart from the β‐barrel the three groups show no close sequence or structural homology but these pores exhibit symmetrical voltage gating when reconstituted into planar lipid bilayers. The structures of several of these are known and many site‐directed mutants have been examined. As a result it seems evident that the gating is a common characteristic of these unrelated large pores and is not generated by specialised structures in the pore lumen.