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Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97

Xuemei Yuan1, Peter Simpson, Ciaran McKeown

  • 1Department of Biological Sciences, Wolfson Laboratories, Imperial College London, South Kensington, London, UK.

The EMBO Journal
|March 19, 2004
PubMed

Insights

The p47 protein

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • p47 is a key adaptor for the AAA ATPase p97, crucial for membrane fusion.
  • The p97-p47 complex regulates Golgi membrane fusion, with p47's ubiquitin recognition being vital.

Purpose of the Study:

  • To determine the high-resolution solution structures of p47's UBA and SEP domains.
  • To characterize the interaction of p47's UBA domain with ubiquitin.
  • To investigate p47 self-association and its regulation by p97.

Main Methods:

  • High-resolution solution structure determination (NMR or SAXS).
  • Biophysical techniques to study protein-protein interactions (e.g., SPR, ITC).
  • Structural analysis of UBA-ubiquitin complex.

Main Results:

  • The N-terminal UBA domain of p47 adopts a canonical three-helix bundle fold.
  • A stable complex structure between the p47 UBA domain and ubiquitin was determined.
  • The central SEP domain of p47 exhibits a novel fold with specific secondary structure arrangement.
  • p47 demonstrates a propensity for self-association, which is inhibited by p97 N-terminal binding.

Conclusions:

  • Structural insights into p47's UBA-ubiquitin interaction and its novel SEP domain fold.
  • Demonstration of p47 self-association and its regulation by p97, suggesting mechanisms for complex assembly.

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