1oz4

From Proteopedia

Revision as of 06:57, 18 November 2007

VCP/p97

Overview

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 Structure

1OZ4 is a Single protein structure of sequence from Mus musculus with ZN, ADP and AF3 as ligands. The following page contains interesting information on the relation of 1OZ4 with [AAA+ Proteases]. Full crystallographic information is available from OCA.

Reference

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

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