Ontology highlight
ABSTRACT:
SUBMITTER: Webby MN
PROVIDER: S-EPMC9629720 | biostudies-literature | 2022 Nov
REPOSITORIES: biostudies-literature
Webby Melissa N MN Oluwole Abraham O AO Pedebos Conrado C Inns Patrick G PG Olerinyova Anna A Prakaash Dheeraj D Housden Nicholas G NG Benn Georgina G Sun Dawei D Hoogenboom Bart W BW Kukura Philipp P Mohammed Shabaz S Robinson Carol V CV Khalid Syma S Kleanthous Colin C
Science advances 20221102 44
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 <i>Escherichia coli</i> 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 ...[more]