Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 20, Issue 11, Pages 1265-U186Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2677
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Funding
- Swiss National Science Foundation [PP00P3_ 128419]
- European Research Commission [MOMP 281764]
- Novartis Foundation
- Werner-Siemens Foundation
- Swiss National Science Foundation (SNF) [PP00P3_128419] Funding Source: Swiss National Science Foundation (SNF)
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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.
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