3cf1
Structure of P97/vcp in complex with ADP/ADP.alfx
OverviewOverview
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-kappa b pathway. Here we present the crystal structure of full-length Mus musculus p97/VCP in complex with a mixture of ADP and ADP-AlF(x) at a resolution of 4.7 A. 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 Zn(2+) occludes the central pore of the hexamer, suggesting that substrate does not thread through the pore of the molecule.
About this StructureAbout this Structure
3CF1 is a Single protein structure of sequence from Mus musculus. This structure supersedes the now removed PDB entry 1yq0. Full crystallographic information is available from OCA.
ReferenceReference
Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains., DeLaBarre B, Brunger AT, Nat Struct Biol. 2003 Oct;10(10):856-63. Epub 2003 Aug 31. PMID:12949490 Page seeded by OCA on Thu Apr 24 09:53:33 2008