Structural highlights
Function
[C9R0N0_ECOD1] Involved in the TonB-independent uptake of proteins (By similarity).[HAMAP-Rule:MF_00671] [CEA9_ECOLX] This plasmid-coded bactericidal protein is an endonuclease active on both single- and double-stranded DNA but with undefined specificity. Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.
Publication Abstract from PubMed
Porins are beta-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. Formation of the translocon involved ColE9's unstructured N-terminal domain threading in opposite directions through two OmpF subunits, capturing its target TolB on the other side of the membrane in a fixed orientation that triggers colicin import. Thus, an intrinsically disordered protein can tunnel through the narrow pores of an oligomeric porin to deliver an epitope signal to the cell to initiate cell death.
Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF.,Housden NG, Hopper JT, Lukoyanova N, Rodriguez-Larrea D, Wojdyla JA, Klein A, Kaminska R, Bayley H, Saibil HR, Robinson CV, Kleanthous C Science. 2013 Jun 28;340(6140):1570-4. doi: 10.1126/science.1237864. PMID:23812713[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Housden NG, Hopper JT, Lukoyanova N, Rodriguez-Larrea D, Wojdyla JA, Klein A, Kaminska R, Bayley H, Saibil HR, Robinson CV, Kleanthous C. Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF. Science. 2013 Jun 28;340(6140):1570-4. doi: 10.1126/science.1237864. PMID:23812713 doi:10.1126/science.1237864
