Dataset Information

XL-MS data of BAM and SurA binding

ABSTRACT: We present XL-MS data of the BAM:SurA complex to define the interaction sites for SurA on BAM

INSTRUMENT(S): Orbitrap Exploris 240

ORGANISM(S): Escherichia Coli

SUBMITTER: Antonio Calabrese

LAB HEAD: Antonio Calabrese

PROVIDER: PXD030209 | Pride | 2022-07-12

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	fbsaca_210814E_08.mgf	Mgf
	fbsaca_210814E_08.zhrm	Other

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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]

PMID: 35676411

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