Molecular mimicry enables competitive recruitment by a natively disordered protein.

Journal article

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...

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Authors: Bonsor, D; Grishkovskaya, I; Dodson, E; Kleanthous, K

• Journal: Journal of the American Chemical Society
• Volume: 129
• Issue: 15
• Pages: 4800-4807
• Publication date: 2007-04-01
• DOI: 10.1021/ja070153n
• EISSN: 1520-5126
• ISSN: 0002-7863
• Language: English
• Keywords: Protein Structure, Quaternary; Peptidoglycan; Amino Acids; Protein Binding; Hydrogen Bonding; Lipoproteins; Periplasmic Proteins; Escherichia coli Proteins; Protein Denaturation; Bacterial Outer Membrane Proteins; Molecular Mimicry; Thermodynamics; Crystallography, X-Ray; Protein Transport; Models, Molecular