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

Xuemei Yuan, Peter Simpson, Ciaran McKeown, Hisao Kondo, Keiji Uchiyama, Russell Wallis, Ingrid Dreveny, Catherine Keetch, Xiaodong Zhang, Carol Robinson, Paul Freemont, Stephen Matthews

Research output: Contribution to journalArticlepeer-review

64 Citations (Scopus)


p47 is a major adaptor molecule of the cytosolic AAA ATPase p97. The principal role of the p97-p47 complex is in regulation of membrane fusion events. Mono-ubiquitin recognition by p47 has also been shown to be crucial in the p97-p47-mediated Golgi membrane fusion events. Here, we describe the high-resolution solution structures of the N-terminal UBA domain and the central domain (SEP) from p47. The p47 UBA domain has the characteristic three-helix bundle fold and forms a highly stable complex with ubiquitin. We report the interaction surfaces of the two proteins and present a structure for the p47 UBA-ubiquitin complex. The p47 SEP domain adopts a novel fold with a βββααβ secondary structure arrangement, where β4 pairs in a parallel fashion to β1. Based on biophysical studies, we demonstrate a clear propensity for the self-association of p47. Furthermore, p97 N binding abolishes p47 self-association, revealing the potential interaction surfaces for recognition of other domains within p97 or the substrate.

Original languageEnglish
Pages (from-to)1463-1473
Number of pages11
JournalEMBO Journal
Issue number7
Publication statusPublished - Apr 7 2004
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General Neuroscience
  • Molecular Biology
  • General Biochemistry,Genetics and Molecular Biology
  • General Immunology and Microbiology


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