细菌外膜
超分子化学
生物物理学
化学
膜
细菌
膜蛋白
大肠杆菌
膜脂
超分子组装
木桶(钟表)
细胞膜
细胞生物学
生物
生物化学
结晶学
材料科学
晶体结构
复合材料
基因
遗传学
作者
Melissa N. Webby,Abraham Olusegun Oluwole,Conrado Pedebos,Patrick George Inns,Anna Olerinyova,Dheeraj Prakaash,Nicholas G. Housden,Georgina Benn,Dawei Sun,Bart W. Hoogenboom,Philipp Kukura,Shabaz Mohammed,Carol V. Robinson,Syma Khalid,Colin Kleanthous
出处
期刊:Science Advances
[American Association for the Advancement of Science (AAAS)]
日期:2022-11-04
卷期号:8 (44)
被引量:20
标识
DOI:10.1126/sciadv.adc9566
摘要
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.
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