1. ABOUT THE DATASET
--------------------

Title:	Dataset for 'Dual client binding sites in the ATP-independent chaperone SurA' [Dataset]. https://doi.org/10.5518/1423

Creator(s): Joel A. Crossley

Organisation(s): [1] Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, United Kingdom

Rights-holder(s):Unless otherwise stated, Copyright 2024 University of Leeds

Publication Year: 2024

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). 

Cite as: Bob Schiffrin*, Joel A. Crossley*, Martin Walko, Jonathan M. Machin, G. Nasir Khan, Iain W. Manfield, Andrew J. Wilson, David J. Brockwell, Tomas Fessl, Antonio N. Calabrese, Sheena E. Radford#, Anastasia Zhuravleva#. (2024): Dataset for 'Dual client binding sites in the ATP-independent chaperone SurA'. [Dataset]. https://doi.org/10.5518/1423.

Contact: j.a.crossley@leeds.ac.uk


2. TERMS OF USE
---------------

[A standard copyright notice and licence statement with URL can be used, e.g. Copyright [publication year] [University of Leeds, name of other rights-holder(s)]. Unless otherwise stated, this dataset is licensed under a Creative Commons Attribution 4.0 International Licence: https://creativecommons.org/licenses/by/4.0/.]


3. PROJECT AND FUNDING INFORMATION
----------------------------------

We acknowledge Wellcome for funding the Chirascan CD spectrometer was (094232/Z/10/Z), the Monolith NT.115 MST (105615/Z/14/Z) and ITC instruments (094232/Z/10/Z). We acknowledge Astbury Biostructrure Laboratory for access to the 950-MHz spectrometer which was funded by the University of Leeds. B.S acknowledges support from the BBSRC (BB/T000635/1). A.N.C. acknowledges the support of a Sir Henry Dale Fellowship jointly funded by Wellcome and the Royal Society (Grant Number 220628/Z/20/Z) and a University Academic Fellowship from the University of Leeds.  S.E.R. holds a Royal Society Professorial Fellowship (RSRP/R1/211057). We acknowledge funding from BBSRC for J.A.C. (BB/T008059/1) and M.W. (BB/ V003577/1). J.M.M. was funded by Wellcome (222373/Z/21/Z). We thank EPSRC (EP/N013573/1) and BBSRC (BB/V003577/1) for funding peptide synthesis. T.F. is supported by the European Regional Development Fund-Project (CZ.02.1.01/0.0/0.0/15_003/0000441) and the Czech Science Foundation (20-11563Y). For the purpose of Open Access, the authors have applied a CC BY public copyright licence to any Author Accepted Manuscript version arising from this submission.

4. CONTENTS
-----------

apo-OmpX.hdf5
OmpX-SurA-WT.hdf5
OmpX-SurA-core.hdf5
apo-OmpX_4M_Urea.hdf5

5. METHODS
----------

Single-molecule Förster resonance energy transfer (smFRET) experiments were performed on a custom-built confocal epi-illuminated microscope in a standard inverted-stage configuration with a pulsed interleaved excitation regime.