Mas et al, Science Advances 6, eabc5822 (2020)
The molecular chaperone Skp transports outer membrane proteins in Gram-negative bacteria. Using NMR spectroscopy, we showed that Skp activity is modulated through a monomer-trimer transition, where the monomeric is unfolded. Native client proteins contact all three subunits simultaneously to trimerize Skp. Skp is a unique example how chaperone activity is regulated as a function of the presence of client proteins.