Cell entry mechanism of enzymatic bacterial colicins: porin recruitment and the thermodynamics of receptor binding.

Journal article

Binding of enzymatic E colicins to the vitamin B12 receptor, BtuB, is the first stage in a cascade of events that culminate in the translocation of the cytotoxic nuclease into the Escherichia coli cytoplasm and release of its tightly bound immunity protein. A dogma of colicin biology is that the toxin coiled-coil connecting its functional domains must unfold or unfurl to span the periplasm, with recent reports claiming this reaction is initiated by receptor binding. We report isothermal titra...

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Authors: Housden, N; Loftus, SR; Moore, G; James, R; Kleanthous, K

• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 102
• Issue: 39
• Pages: 13849-13854
• Publication date: 2005-09-01
• DOI: 10.1073/pnas.0503567102
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Escherichia coli; Escherichia coli Proteins; Receptors, Peptide; Colicins; Protein Transport; Protein Structure, Tertiary; Bacterial Outer Membrane Proteins; Sequence Deletion; Protein Folding; Membrane Transport Proteins; Disulfides; Calcium; Thermodynamics; Porins