Structure of the AAA ATPase p97.

@article{Zhang2000StructureOT,
  title={Structure of the AAA ATPase p97.},
  author={Xiaoming Zhang and Anthony A. Shaw and Paul A. Bates and Richard H. Newman and Brent E. Gowen and Evgenija Orlova and Michael A. Gorman and Hisao Kondo and Pawel Dokurno and John M. Lally and Gordon A. Leonard and Herbert b. Meyer and Marin van Heel and Paul S. Freemont},
  journal={Molecular cell},
  year={2000},
  volume={6 6},
  pages={
          1473-84
        }
}
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 murine p97 at 2.9 A resolution, and a cryoelectron microscopy structure of full-length rat p97 at 18 A resolution. Together, these structures show that the D1 and D2 hexamers pack in a tail-to-tail arrangement, and… CONTINUE READING
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