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Data for 'Dual client binding sites in the ATP-independent chaperone SurA'

Citation

Schiffrin, Bob and Crossley, Joel A. (2024) Data for 'Dual client binding sites in the ATP-independent chaperone SurA'. University of Leeds. [Dataset] https://doi.org/10.5518/1423

Dataset description

The ATP-independent chaperone SurA protects unfolded outer membrane proteins (OMPs) from aggregation in the periplasm of Gram-negative bacteria and delivers them to the beta-barrel assembly machinery (BAM) for folding into the outer membrane (OM). Precisely how SurA recognises and binds its different OMP clients remains unclear. E. coli SurA comprises three domains: a core and two PPIase domains (P1 and P2). Here, we present single-molecule Förster resonance energy transfer (smFRET) data showing conformational changes of unfolded OmpX (apo-OmpX.hdf5) when bound to SurA wild-type (OmpX+SurA-WT.hdf5), the SurA core domain (OmpX+SurA-core.hdf5) and finally, in 4 M urea (apo-OmpX_4M_Urea.hdf5).

Keywords: NMR, smFRET, SurA, OmpX, OMP, chaperones.
Subjects: C000 - Biological sciences
Divisions: Faculty of Biological Sciences > Astbury Centre for Structural Molecular Biology
Faculty of Biological Sciences > School of Molecular and Cellular Biology
License: Creative Commons Attribution 4.0 International (CC BY 4.0)
Date deposited: 06 Aug 2024 16:00
URI: https://archive.researchdata.leeds.ac.uk/id/eprint/1310

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