OmpF
From Proteopedia
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OmpF complex with colicin peptide and beta-octylglucoside, 3o0e | |||||||
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Ligands: | |||||||
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Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||
Coordinates: | save as pdb, mmCIF, xml |
OmpF is a major outer membrane porin found in E. coli. Mutations in the ompF gene result in a reduced sensitivity of the E. coli cell to proteins such as Colicins, and also bacteriophages[1].
OmpF production is regulated by OmpR, a protein that is phosphorylated by EnvZ to induce DNA binding to the promotor region of OmpF, and repress transcription of OmpF[2][3].
This structure shows a monomer of , bound to a of a region of the translocation domain of Colicin E9.
3D structures of porin
References
- ↑ Lavina M, Pugsley AP, Moreno F. Identification, mapping, cloning and characterization of a gene (sbmA) required for microcin B17 action on Escherichia coli K12. J Gen Microbiol. 1986 Jun;132(6):1685-93. PMID:3543211
- ↑ Forst S, Delgado J, Inouye M. Phosphorylation of OmpR by the osmosensor EnvZ modulates expression of the ompF and ompC genes in Escherichia coli. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6052-6. PMID:2668953
- ↑ Forst SA, Delgado J, Inouye M. DNA-binding properties of the transcription activator (OmpR) for the upstream sequences of ompF in Escherichia coli are altered by envZ mutations and medium osmolarity. J Bacteriol. 1989 Jun;171(6):2949-55. PMID:2656631