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| Title | Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p. |
|---|---|
| Journal, issue, pages | J Mol Biol, Vol. 377, Issue 2, Page 352-363, Year 2008 |
| Publish date | Mar 21, 2008 |
 Authors | Claudia Hartmann / Mohamed Chami / Ulrich Zachariae / Bert L de Groot / Andreas Engel / Markus G Grütter /  |
| 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 ...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. |
 External links | J Mol Biol / PubMed:18272179 |
| Methods | EM (single particle) / X-ray diffraction |
| Resolution | 3.35 - 18.0 Å |
| Structure data |  EMDB-1481:  PDB-2rko: |
| Source |
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 Keywords |  PROTEIN TRANSPORT / AAA-ATPase domain / ATP-binding / Endosome / Membrane / Nucleotide-binding / Phosphorylation / Transport |
