Biochemistry and regulation of a novel Escherichia coli K-12 porin protein, OmpG, which produces unusually large channels.

ABSTRACT: A novel porin, OmpG, is produced in response to a chromosomal mutation termed cog-192. Molecular characterization of cog-192 revealed that it is a large chromosomal deletion extending from the 3' end of pspA through to the 5' end of an open reading frame located immediately upstream of ompG. As a result of this 13.1-kb deletion, the expression of ompG was placed under the control of the pspA promoter. Characterization of OmpG revealed that it is quite different from other porins. Proteoliposome swelling assays showed that OmpG channels were much larger than those of the OmpF and OmpC porins, with an estimated limited diameter of about 2 nm. The channel lacked any obvious solute specificity. The folding model of OmpG suggests that it is the first 16-stranded beta-barrel porin that lacks the

SUBMITTER: Fajardo DA 

PROVIDER: S-EPMC107454 | biostudies-literature | 1998 Sep

REPOSITORIES: biostudies-literature