2RKO

Crystal Structure of the Vps4p-dimer

Summary for 2RKO

• Entry DOI: 10.2210/pdb2rko/pdb
• Related: 1XWI
• Descriptor: Vacuolar protein sorting-associated protein 4 (1 entity in total)
• Functional Keywords: aaa-atpase domain, atp-binding, endosome, membrane, nucleotide-binding, phosphorylation, protein transport, transport
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Endosome membrane; Peripheral membrane protein (By similarity): P52917
• Total number of polymer chains: 1
• Total formula weight: 36647.42

Authors

Hartmann, C.,Gruetter, M.G. (deposition date: 2007-10-17, release date: 2008-02-26, Last modification date: 2023-10-25)

Primary citation

Hartmann, C.,Chami, M.,Zachariae, U.,de Groot, B.L.,Engel, A.,Gruetter, M.G.
Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p
J.Mol.Biol., 377:352-363, 2008

PubMed Abstract: The vacuolar protein sorting (Vps) pathway, in which Vps4 class I AAA-ATPases play a central role, regulates growth factor receptors, immune response, and developmental signaling, and participates in tumor suppression, apoptosis, and retrovirus budding. We present the first atomic structure of the nucleotide-free yeast His(6)DeltaNVps4p dimer and its AMPPNP (5'-adenylyl-beta,gamma-imidodiphosphate)-bound tetradecamer, derived from a cryo electron microscopy map. Vps4p dimers form two distinct heptameric rings and accommodate AAA cassettes in a head-to-head--not in a head-to-tail-fashion as in class II AAA-ATPases. Our model suggests a mechanism for disassembling ESCRT (endosomal sorting complex required for transport) complexes by movements of substrate-binding domains located at the periphery of the tetradecamer during ATP hydrolysis in one ring, followed by translocation through the central pore and ATP hydrolysis in the second ring.

PubMed: 18272179
DOI: 10.1016/j.jmb.2008.01.010

Experimental method

X-RAY DIFFRACTION (3.35 Å)