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Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.
Journal article

Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.

  • 2013-10-01
Published in:
  • 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
English 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.
Language
  • English
Open access status
closed
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Persistent URL
https://sonar.ch/global/documents/232142
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