Dataset Information
Identification of SurA inter-domain dynamics and client binding by XL-MS
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Synapt MS, Q Exactive
ORGANISM(S): Escherichia Coli
SUBMITTER: 
Antonio Calabrese
LAB HEAD: Sheena E Radford
PROVIDER: PXD016993 | Pride | 2020-05-22
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| I79C_Enrich.mgf | Mgf | |||
| I79C_Gel.mgf | Mgf | |||
| I79C_Gel1.mgf | Mgf | |||
| K99C_Enrich.mgf | Mgf | |||
| K99C_Gel.mgf | Mgf |
Items per page: 1 - 5 of 33 |
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]
