Colicin N binds to the periphery of its receptor and translocator, outer membrane protein F
| Autor: | Matthew J. Conroy, Jeremy H. Lakey, Per A. Bullough, Katrina Gill, Helen Ridley, Virak Visudtiphole, Thomas G. Baboolal |
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| Rok vydání: | 2007 |
| Předmět: |
Lipopolysaccharides
Models Molecular PROTEINS Membrane lipids Colicins Porins Electrons Receptors Cell Surface Plasma protein binding Biology Binding Competitive Models Biological Article 03 medical and health sciences Membrane Lipids Structural Biology Binding site Molecular Biology 030304 developmental biology 0303 health sciences Binding Sites Escherichia coli Proteins 030302 biochemistry & molecular biology technology industry and agriculture Membrane transport biochemical phenomena metabolism and nutrition Transport protein Protein Structure Tertiary Protein Transport Biochemistry SIGNALING Colicin Porin Biophysics bacteria lipids (amino acids peptides and proteins) Bacterial outer membrane Crystallization Dimerization Protein Binding |
| Zdroj: | Structure(London, England:1993) |
| ISSN: | 0969-2126 |
| Popis: | Summary Colicins kill Escherichia coli after translocation across the outer membrane. Colicin N displays an unusually simple translocation pathway, using the outer membrane protein F (OmpF) as both receptor and translocator. Studies of this binary complex may therefore reveal a significant component of the translocation pathway. Here we show that, in 2D crystals, colicin is found outside the porin trimer, suggesting that translocation may occur at the protein-lipid interface. The major lipid of the outer leaflet interface is lipopolysaccharide (LPS). It is further shown that colicin N binding displaces OmpF-bound LPS. The N-terminal helix of the pore-forming domain, which is not required for pore formation, rearranges and binds to OmpF. Colicin N also binds artificial OmpF dimers, indicating that trimeric symmetry plays no part in the interaction. The data indicate that colicin is closely associated with the OmpF-lipid interface, providing evidence that this peripheral pathway may play a role in colicin transmembrane transport. |
| Databáze: | OpenAIRE |
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