Dataset Information
Inter-domain dynamics in the chaperone SurA and multi-site binding to its unfolded outer membrane protein clients revealed by HDX-MS
Ontology highlight
ABSTRACT:
INSTRUMENT(S):
ORGANISM(S): Escherichia Coli
SUBMITTER: 
Antonio Calabrese
LAB HEAD: Sheena E. Radford
PROVIDER: PXD017010 | Pride | 2020-05-22
REPOSITORIES: Pride
Dataset's files
| 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
Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.
Nature communications 20200501 1
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]