2rkl

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Revision as of 08:55, 23 January 2008

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spinqualitylabelsall models 2rkl, resolution 1.500Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of S.cerevisiae Vta1 C-terminal domain

Overview

The MVB pathway plays essential roles in several eukaryotic cellular, processes. Proper function of the MVB pathway requires reversible membrane, association of the ESCRTs, a process catalyzed by Vps4 ATPase. Vta1, regulates the Vps4 activity, but its mechanism of action was poorly, understood. We report the high-resolution crystal structures of the Did2-, and Vps60-binding N-terminal domain and the Vps4-binding C-terminal domain, of S. cerevisiae Vta1. The C-terminal domain also mediates Vta1, dimerization and both subunits are required for its function as a Vps4, regulator. Emerging from our analysis is a mechanism of regulation by Vta1, in which the C-terminal domain stabilizes the ATP-dependent double ring, assembly of Vps4. In addition, the MIT motif-containing N-terminal domain, projected by a long disordered linker, allows contact between the Vps4, disassembly machinery and the accessory ESCRT-III proteins. This provides, an additional level of regulation and coordination for ESCRT-III assembly, and disassembly.

About this Structure

2RKL is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structural basis of vta1 function in the multivesicular body sorting pathway., Xiao J, Xia H, Zhou J, Azmi IF, Davies BA, Katzmann DJ, Xu Z, Dev Cell. 2008 Jan;14(1):37-49. PMID:18194651

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