Research Data Leeds Repository
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/10.5518/14231
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. | ||||||
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Subjects: | C000 - Biological sciences2 | ||||||
Divisions: | Faculty of Biological Sciences > Astbury Centre for Structural Molecular Biology3 Faculty of Biological Sciences > School of Molecular and Cellular Biology4 |
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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/13107 | ||||||
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Documentation
Data
- 1. https://doi.org/10.5518/1423
- 2. https://archive.researchdata.leeds.ac.uk/view/subjects/C000.html
- 3. https://archive.researchdata.leeds.ac.uk/view/divisions/ACSMB/
- 4. https://archive.researchdata.leeds.ac.uk/view/divisions/SMCB/
- 5. https://doi.org/10.1038/s41467-024-52021-1
- 6. https://eprints.whiterose.ac.uk/216546/
- 7. https://archive.researchdata.leeds.ac.uk/id/eprint/1310
- 8. https://orcid.org/0000-0002-1670-7356
- 9. https://orcid.org/0000-0002-6656-1578
- 10. mailto:j.a.crossley@leeds.ac.uk
- 11. https://archive.researchdata.leeds.ac.uk/1310/5/readme_Crossley_2024.txt
- 12. https://archive.researchdata.leeds.ac.uk/1310/5/readme_Crossley_2024.txt
- 13. https://archive.researchdata.leeds.ac.uk/1310/5/readme_Crossley_2024.txt
- 14. https://archive.researchdata.leeds.ac.uk/1310/5/readme_Crossley_2024.txt
- 15. https://archive.researchdata.leeds.ac.uk/1310/1/apo-OmpX.hdf5
- 16. https://archive.researchdata.leeds.ac.uk/1310/1/apo-OmpX.hdf5
- 17. https://archive.researchdata.leeds.ac.uk/1310/1/apo-OmpX.hdf5
- 18. https://archive.researchdata.leeds.ac.uk/1310/1/apo-OmpX.hdf5
- 19. https://archive.researchdata.leeds.ac.uk/1310/2/apo-OmpX_4M_Urea.hdf5
- 20. https://archive.researchdata.leeds.ac.uk/1310/2/apo-OmpX_4M_Urea.hdf5
- 21. https://archive.researchdata.leeds.ac.uk/1310/2/apo-OmpX_4M_Urea.hdf5
- 22. https://archive.researchdata.leeds.ac.uk/1310/2/apo-OmpX_4M_Urea.hdf5
- 23. https://archive.researchdata.leeds.ac.uk/1310/3/OmpX-SurA-core.hdf5
- 24. https://archive.researchdata.leeds.ac.uk/1310/3/OmpX-SurA-core.hdf5
- 25. https://archive.researchdata.leeds.ac.uk/1310/3/OmpX-SurA-core.hdf5
- 26. https://archive.researchdata.leeds.ac.uk/1310/3/OmpX-SurA-core.hdf5
- 27. https://archive.researchdata.leeds.ac.uk/1310/4/OmpX-SurA-WT.hdf5
- 28. https://archive.researchdata.leeds.ac.uk/1310/4/OmpX-SurA-WT.hdf5
- 29. https://archive.researchdata.leeds.ac.uk/1310/4/OmpX-SurA-WT.hdf5
- 30. https://archive.researchdata.leeds.ac.uk/1310/4/OmpX-SurA-WT.hdf5