Lipids mediate supramolecular outer membrane protein assembly in bacteria.
Lipids mediate supramolecular outer membrane protein assembly in bacteria.
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DOI:
10.1126/sciadv.adc9566
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发表时间:
2022-11-04
期刊:
影响因子:
13.6
通讯作者:
中科院分区:
文献类型:
--
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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. Lipids tether functionally-diverse proteins together creating complexes that maintain stability of the bacterial outer membrane.
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