Burmann BM Wang C Hiller S 2013 The biogenesis of integral outer-membrane proteins (OMPs) in Gram-negative bacteria requires molecular chaperones that prevent the aggregation of OMP polypeptides in the aqueous periplasmic space. How these energy-independent chaperones interact with their substrates is not well understood. We have used high-resolution NMR spectroscopy to examine the conformation and dynamics of the Escherichia coli periplasmic chaperone Skp and two of its complexes with OMPs. The Skp trimer constitutes a flexible architectural scaffold that becomes more rigid upon substrate binding. The OMP substrates populate a dynamic conformational ensemble with structural interconversion rates on the submillisecond timescale. The global lifetime of the chaperone-substrate complex is seven orders of magnitude longer, emerging from the short local lifetimes by avidity. The dynamic state allows for energy-independent substrate release and provides a general paradigm for the conformation of OMP polypeptides bound to energy-independent chaperones. https://sonar.ch/global/documents/232142 eng info:eu-repo/semantics/altIdentifier/doi/10.1038/nsmb.2677 info:eu-repo/semantics/altIdentifier/pmid/24077225 Nature structural & molecular biology. - 2013 Bacterial Outer Membrane Proteins DNA-Binding Proteins Escherichia coli Escherichia coli Proteins Hydrolases Magnetic Resonance Spectroscopy Models, Biological Models, Molecular Molecular Chaperones Molecular Dynamics Simulation Protein Conformation Time Factors Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp. http://purl.org/coar/resource_type/c_6501