2RKK

Crystal Structure of S.cerevisiae Vta1 N-terminal domain

Summary for 2RKK

• Entry DOI: 10.2210/pdb2rkk/pdb
• Related: 2RKL
• Descriptor: Vacuolar protein sorting-associated protein VTA1 (2 entities in total)
• Functional Keywords: mit motif, cytoplasm, endosome, lipid transport, membrane, protein transport, transport
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm : Q06263
• Total number of polymer chains: 2
• Total formula weight: 38298.25

Authors

Xiao, J.,Xia, H.,Zhou, J.,Xu, Z. (deposition date: 2007-10-16, release date: 2008-01-22, Last modification date: 2024-02-21)

Primary citation

Xiao, J.,Xia, H.,Zhou, J.,Azmi, I.F.,Davies, B.A.,Katzmann, D.J.,Xu, Z.
Structural basis of vta1 function in the multivesicular body sorting pathway.
Dev.Cell, 14:37-49, 2008

PubMed Abstract: 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.

PubMed: 18194651
DOI: 10.1016/j.devcel.2007.10.013

Experimental method

X-RAY DIFFRACTION (2.9 Å)