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Related Experiment Videos

Conformational changes in the AAA ATPase p97-p47 adaptor complex.

Fabienne Beuron1, Ingrid Dreveny, Xuemei Yuan

  • 1Centre for Structural Biology, Division of Molecular Biosciences, Imperial College London, South Kensington, UK.

The EMBO Journal
|April 8, 2006
PubMed
Summary
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The AAA+ ATPase p97/VCP, with adaptor p47, plays key roles in cell functions. Structural studies reveal how nucleotide states alter p47 arrangement on p97, impacting protein complex disassembly.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • The AAA+ ATPase p97/VCP is crucial for cellular processes like protein degradation and organelle reassembly.
  • Adaptor proteins, such as p47, are essential for p97 function in membrane fusion and other events.

Purpose of the Study:

  • To determine the three-dimensional structures of p97 in complex with its adaptor p47 in different nucleotide states.
  • To elucidate the mechanism of ATP-dependent conformational changes in p97 and its impact on p47 binding and function.

Main Methods:

  • Three-dimensional cryo-electron microscopy (cryo-EM) at ~20 Angstrom resolution.
  • Nuclear Magnetic Resonance (NMR) spectroscopy and other biophysical measurements.

Main Results:

Related Experiment Videos

  • The study resolved structures of the hexameric p97-p47 complex in two distinct nucleotide-bound states.
  • Distinct arrangements of the p47 trimer on the p97 hexamer were observed, correlating with nucleotide state.
  • A model for ATP-dependent p97 N-domain motions and subsequent p47 domain rearrangement was proposed.

Conclusions:

  • The findings provide insights into the allosteric regulation of p97 activity by adaptor proteins.
  • The proposed model explains how nucleotide-dependent conformational changes drive p97 function, including target complex disassembly.