Ontology highlight
ABSTRACT:
INSTRUMENT(S): Synapt MS
ORGANISM(S): Escherichia Coli
SUBMITTER: Antonio Calabrese
LAB HEAD: Antonio Calabrese
PROVIDER: PXD030268 | Pride | 2022-07-12
REPOSITORIES: Pride
Action | DRS | |||
---|---|---|---|---|
BamA.DnX | Other | |||
BamBC.DnX | Other | |||
BamDE.DnX | Other | |||
SurABAM_190710.DnX | Other | |||
fbsaca_190710_1_02.raw.zip | Raw |
Items per page: 1 - 5 of 110 |
Communications biology 20220608 1
Correct folding of outer membrane proteins (OMPs) into the outer membrane of Gram-negative bacteria depends on delivery of unfolded OMPs to the β-barrel assembly machinery (BAM). How unfolded substrates are presented to BAM remains elusive, but the major OMP chaperone SurA is proposed to play a key role. Here, we have used hydrogen deuterium exchange mass spectrometry (HDX-MS), crosslinking, in vitro folding and binding assays and computational modelling to show that the core domain of SurA and ...[more]