Structure of the AAA ATPase p97

Xiaodong Zhang, Anthony Shaw, Paul A. Bates, Richard H. Newman, Brent Gowen, Elena Orlova, Michael A. Gorman, Hisao Kondo, Pawel Dokurno, John Lally, Gordon Leonard, Hemmo Meyer, Marin Van Heel, Paul S. Freemont

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393 Citations (Scopus)


p97, an abundant hexameric ATPase of the AAA family, is involved in homotypic membrane fusion. It is thought to disassemble SNARE complexes formed during the process of membrane fusion. Here, we report two structures: A crystal structure of the N-terminal and D1 ATPase domains of routine p97 at 2.9 Å resolution, and a cryoelectron microscopy structure of full-length rat p97 at 18 Å resolution. Together, these structures show that the D1 and D2 hexamers pack in a tail-totail arrangement, and that the N domain is flexible. A comparison with NSF D2 (ATP complex) reveals possible conformational changes induced by ATP hydrolysis. Given the D1 and D2 packing arrangement, we propose a ratchet mechanism for p97 during its ATP hydrolysis cycle.

Original languageEnglish
Pages (from-to)1473-1484
Number of pages12
JournalMolecular Cell
Issue number6
Publication statusPublished - 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


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