First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
|2rkl, resolution 1.50Å ()|
|Gene:||VTA1 (Saccharomyces cerevisiae)|
Crystal Structure of S.cerevisiae Vta1 C-terminal domain
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Xiao J, Xia H, Zhou J, Azmi IF, Davies BA, Katzmann DJ, Xu Z. Structural basis of Vta1 function in the multivesicular body sorting pathway. Dev Cell. 2008 Jan;14(1):37-49. PMID:18194651 doi:10.1016/j.devcel.2007.10.013
Page seeded by OCA on Wed Feb 18 06:49:27 2009