Proteomics

Dataset Information

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Inter-domain dynamics in the chaperone SurA and multi-site binding to its unfolded outer membrane protein clients revealed by HDX-MS

ABSTRACT: We present HDX-MS data of apo-SurA, SurA in complex with OmpX, OmpF and a peptide with sequence WEYIPNV to define (1) interdomain dynamics in the periplasmic chaperone SurA, and (2) the binding site of OmpX, OmpF and WEYIPNV on SurA.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Escherichia Coli

SUBMITTER: Antonio Calabrese  

LAB HEAD: Sheena E. Radford

PROVIDER: PXD017010 | Pride | 2020-05-22

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
SurAOMPs.DnX Other
SurAOmpF_02.raw.zip Raw
SurAOmpF_03.raw.zip Raw
SurAOmpF_04.raw.zip Raw
SurAOmpF_05.raw.zip Raw
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Publications

The periplasmic chaperone SurA plays a key role in outer membrane protein (OMP) biogenesis. E. coli SurA comprises a core domain and two peptidylprolyl isomerase domains (P1 and P2), but its mechanisms of client binding and chaperone function have remained unclear. Here, we use chemical cross-linking, hydrogen-deuterium exchange mass spectrometry, single-molecule FRET and molecular dynamics simulations to map the client binding site(s) on SurA and interrogate the role of conformational dynamics  ...[more]

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