Bonsor, D.A., Grishkovskaya, I., Dodson, E.J. and Kleanthous, C. (2007) Molecular mimicry enables competitive recruitment by a natively disordered protein. Journal of the American Chemical Society, 129 (15). pp. 4800-4807. ISSN 0002-7863Full text not available from this repository.
We report the crystal structure of the Escherichia coli TolB-Pal complex, a protein−protein complex involved in maintaining the integrity of the outer membrane (OM) in all Gram-negative bacteria that is parasitized by colicins (protein antibiotics) to expedite their entry into cells. Nuclease colicins competitively recruit TolB using their natively disordered regions (NDRs) to disrupt its complex with Pal, which is thought to trigger translocation of the toxin across a locally destabilized OM. The structure shows induced-fit binding of peptidoglycan-associated lipoprotein (Pal) to the β-propeller domain of TolB causing the N-terminus of one of its α-helices to unwind and several residues to undergo substantial changes in conformation. The resulting interactions with TolB are known to be essential for the stability of the complex and the bacterial OM. Structural comparisons with a TolB-colicin NDR complex reveal that colicins bind at the Pal site, mimicking rearranged Pal residues while simultaneously appearing to block induced-fit changes in TolB. The study therefore explains how colicins recruit TolB in the bacterial periplasm and highlights a novel binding mechanism for a natively disordered protein.
|Academic Units:||The University of York > Biology (York)|
|Depositing User:||York RAE Import|
|Date Deposited:||03 Apr 2009 11:24|
|Last Modified:||03 Apr 2009 11:24|
|Publisher:||ACS American Chemical Society|
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