6VME
Human ESCRT-I heterotetramer headpiece
Summary for 6VME
| Entry DOI | 10.2210/pdb6vme/pdb |
| Descriptor | Tumor susceptibility gene 101 protein, Vacuolar protein sorting-associated protein 37B, Multivesicular body subunit 12A, ... (5 entities in total) |
| Functional Keywords | endosomal transport, hiv release, macroautophagy, protein transport |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 24 |
| Total formula weight | 204222.14 |
| Authors | Flower, T.G.,Hurley, J.H.,Tjahjono, N. (deposition date: 2020-01-27, release date: 2020-05-20, Last modification date: 2023-10-11) |
| Primary citation | Flower, T.G.,Takahashi, Y.,Hudait, A.,Rose, K.,Tjahjono, N.,Pak, A.J.,Yokom, A.L.,Liang, X.,Wang, H.G.,Bouamr, F.,Voth, G.A.,Hurley, J.H. A helical assembly of human ESCRT-I scaffolds reverse-topology membrane scission. Nat.Struct.Mol.Biol., 27:570-580, 2020 Cited by PubMed Abstract: The ESCRT complexes drive membrane scission in HIV-1 release, autophagosome closure, multivesicular body biogenesis, cytokinesis, and other cell processes. ESCRT-I is the most upstream complex and bridges the system to HIV-1 Gag in virus release. The crystal structure of the headpiece of human ESCRT-I comprising TSG101-VPS28-VPS37B-MVB12A was determined, revealing an ESCRT-I helical assembly with a 12-molecule repeat. Electron microscopy confirmed that ESCRT-I subcomplexes form helical filaments in solution. Mutation of VPS28 helical interface residues blocks filament formation in vitro and autophagosome closure and HIV-1 release in human cells. Coarse-grained (CG) simulations of ESCRT assembly at HIV-1 budding sites suggest that formation of a 12-membered ring of ESCRT-I molecules is a geometry-dependent checkpoint during late stages of Gag assembly and HIV-1 budding and templates ESCRT-III assembly for membrane scission. These data show that ESCRT-I is not merely a bridging adaptor; it has an essential scaffolding and mechanical role in its own right. PubMed: 32424346DOI: 10.1038/s41594-020-0426-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.19 Å) |
Structure validation
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