Journal
NATURE STRUCTURAL BIOLOGY
Volume 10, Issue 10, Pages 856-863Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsb972
Keywords
-
Ask authors/readers for more resources
The ATPase p97/VCP affects multiple events within the cell. These events include the alteration of both nuclear and mitotic Golgi membranes, the dislocation of ubiquitylated proteins from the endoplasmic reticulum and regulation of the NF-kappab pathway. Here we present the crystal structure of full-length Mus musculus p97/VCP in complex with a mixture of ADP and ADP-AlFx at a resolution of 4.7 Angstrom. This is the first complete hexameric structure of a protein containing tandem AAA ( ATPases associated with a variety of cellular activities) domains. Comparison of the crystal structure and cryo-electron microscopy ( EM) reconstructions reveals large conformational changes in the helical subdomains during the hydrolysis cycle. Structural and functional data imply a communication mechanism between the AAA domains. A Zn2+ occludes the central pore of the hexamer, suggesting that substrate does not thread through the pore of the molecule.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available