5XMI
Cryo-EM Structure of the ATP-bound VPS4 mutant-E233Q hexamer (masked)
Summary for 5XMI
| Entry DOI | 10.2210/pdb5xmi/pdb |
| EMDB information | 6733 |
| Descriptor | Vacuolar protein sorting-associated protein 4, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total) |
| Functional Keywords | atpase, eescrtiii, protein transport, vps4 |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 6 |
| Total formula weight | 291929.10 |
| Authors | |
| Primary citation | Sun, S.,Li, L.,Yang, F.,Wang, X.,Fan, F.,Yang, M.,Chen, C.,Li, X.,Wang, H.W.,Sui, S.F. Cryo-EM structures of the ATP-bound Vps4(E233Q) hexamer and its complex with Vta1 at near-atomic resolution Nat Commun, 8:16064-16064, 2017 Cited by PubMed Abstract: The cellular ESCRT-III (endosomal sorting complex required for transport-III) and Vps4 (vacuolar protein sorting 4) comprise a common machinery that mediates a variety of membrane remodelling events. Vps4 is essential for the machinery function by using the energy from ATP hydrolysis to disassemble the ESCRT-III polymer into individual proteins. Here, we report the structures of the ATP-bound Vps4 hexamer and its complex with the cofactor Vta1 (vps twenty associated 1) at resolutions of 3.9 and 4.2 Å, respectively, determined by electron cryo-microscopy. Six Vps4 subunits in both assemblies exhibit a spiral-shaped ring-like arrangement. Locating at the periphery of the hexameric ring, Vta1 dimer bridges two adjacent Vps4 subunits by two different interaction modes to promote the formation of the active Vps4 hexamer during ESCRT-III filament disassembly. The structural findings, together with the structure-guided biochemical and single-molecule analyses, provide important insights into the process of the ESCRT-III polymer disassembly by Vps4. PubMed: 28714467DOI: 10.1038/ncomms16064 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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