Proteomics

Dataset Information

0

HDX-MS data of BAM and SurA binding

ABSTRACT: We present HDX-MS data of the BAM:SurA complex to define the interaction sites for SurA on BAM and vice versa.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Escherichia Coli

SUBMITTER: Antonio Calabrese  

LAB HEAD: Antonio Calabrese

PROVIDER: PXD030268 | Pride | 2022-07-12

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
BamA.DnX Other
BamBC.DnX Other
BamDE.DnX Other
SurABAM_190710.DnX Other
fbsaca_190710_1_02.raw.zip Raw
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Publications

Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding.

Schiffrin Bob B   Machin Jonathan M JM   Karamanos Theodoros K TK   Zhuravleva Anastasia A   Brockwell David J DJ   Radford Sheena E SE   Calabrese Antonio N AN  

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]

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