Ontology highlight
ABSTRACT:
SUBMITTER: Lee J
PROVIDER: S-EPMC4978274 | biostudies-literature | 2016 Aug
REPOSITORIES: biostudies-literature
Lee James J Xue Mingyu M Wzorek Joseph S JS Wu Tao T Grabowicz Marcin M Gronenberg Luisa S LS Sutterlin Holly A HA Davis Rebecca M RM Ruiz Natividad N Silhavy Thomas J TJ Kahne Daniel E DE
Proceedings of the National Academy of Sciences of the United States of America 20160720 31
The assembly of β-barrel proteins into membranes is mediated by an evolutionarily conserved machine. This process is poorly understood because no stable partially folded barrel substrates have been characterized. Here, we slowed the folding of the Escherichia coli β-barrel protein, LptD, with its lipoprotein plug, LptE. We identified a late-stage intermediate in which LptD is folded around LptE, and both components interact with the two essential β-barrel assembly machine (Bam) components, BamA ...[more]