2rkk
From Proteopedia
(New page: 200px<br /><applet load="2rkk" size="350" color="white" frame="true" align="right" spinBox="true" caption="2rkk, resolution 2.900Å" /> '''Crystal Structure o...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The MVB pathway plays essential roles in several eukaryotic cellular | + | 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== | ==About this Structure== | ||
| Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | Structural basis of | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18194651 18194651] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 25: | Line 25: | ||
[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:48:05 2008'' |
Revision as of 16:48, 21 February 2008
|
Crystal Structure of S.cerevisiae Vta1 N-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
2RKK is a Single protein structure of sequence from Saccharomyces cerevisiae. 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
Page seeded by OCA on Thu Feb 21 18:48:05 2008
Categories: Saccharomyces cerevisiae | Single protein | Xia, H. | Xiao,J. | Xu, Z. | Zhou, J. | Cytoplasm | Endosome | Lipid transport | Membrane | Mit motif | Protein transport | Transport
