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

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).