APA
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Webby, M. N., Oluwole, A., Pedebos, C., Inns, P., Olerinyova, A., Prakaash, D., … Kleanthous, C. (2022). Lipids mediate supramolecular outer membrane protein assembly in bacteria. Science Advances.
Chicago/Turabian
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Webby, M. N., A. Oluwole, Conrado Pedebos, P. Inns, Anna Olerinyova, Dheeraj Prakaash, N. G. Housden, et al. “Lipids Mediate Supramolecular Outer Membrane Protein Assembly in Bacteria.” Science Advances (2022).
MLA
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Webby, M. N., et al. “Lipids Mediate Supramolecular Outer Membrane Protein Assembly in Bacteria.” Science Advances, 2022.
BibTeX Click to copy
@article{m2022a,
title = {Lipids mediate supramolecular outer membrane protein assembly in bacteria},
year = {2022},
journal = {Science Advances},
author = {Webby, M. N. and Oluwole, A. and Pedebos, Conrado and Inns, P. and Olerinyova, Anna and Prakaash, Dheeraj and Housden, N. G. and Benn, Georgina and Sun, Dawei and Hoogenboom, B. and Kukura, P. and Mohammed, S. and Robinson, C. and Khalid, S. and Kleanthous, C.}
}
β Barrel outer membrane proteins (OMPs) cluster into supramolecular assemblies that give function to the outer membrane (OM) of Gram-negative bacteria. How such assemblies form is unknown. Here, through photoactivatable cross-linking into the Escherichia coli OM, coupled with simulations, and biochemical and biophysical analysis, we uncover the basis for OMP clustering in vivo. OMPs are typically surrounded by an annular shell of asymmetric lipids that mediate higher-order complexes with neighboring OMPs. OMP assemblies center on the abundant porins OmpF and OmpC, against which low-abundance monomeric β barrels, such as TonB-dependent transporters, are packed. Our study reveals OMP-lipid-OMP complexes to be the basic unit of supramolecular OMP assembly that, by extending across the entire cell surface, couples the requisite multifunctionality of the OM to its stability and impermeability.