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Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

DOI: 10.1126/science.1237864 DOI Help
PMID: 23812713 PMID Help

Authors: N. G. Housden (University of Oxford) , J. T. S. Hopper (University of Oxford) , N. Lukoyanova (Birkbeck College) , D. Rodriguez-larrea (University of Oxford) , J. A. Wojdyla (University of Oxford) , A. Klein (University of Oxford) , R. Kaminska (University of Oxford) , H. Bayley (University of Oxford) , H. R. Saibil (Birkbeck College) , C. V. Robinson (University of Oxford) , C. Kleanthous (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Science , VOL 340 (6140) , PAGES 1570 - 1574

State: Published (Approved)
Published: June 2013

Abstract: Porins are β-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.

Journal Keywords: Colicins; Escherichia; Periplasmic; Porins; Protein; Tertiary; Protein Transport

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography