3FRV
Structure of Human CHMP3 (residues 1-150)
Summary for 3FRV
| Entry DOI | 10.2210/pdb3frv/pdb |
| Related | 3FRR 3FRS 3FRT |
| Descriptor | Charged multivesicular body protein 3 (1 entity in total) |
| Functional Keywords | escrt, escrt-iii, chmp, ist1, coiled coil, cytoplasm, lipoprotein, membrane, myristate, phosphoprotein, protein transport, transport |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm, cytosol: Q9Y3E7 |
| Total number of polymer chains | 1 |
| Total formula weight | 17408.70 |
| Authors | Hill, C.P.,Schubert, H.L.,McCullough, J.,Sundquist, W.I. (deposition date: 2009-01-08, release date: 2009-06-30, Last modification date: 2023-09-06) |
| Primary citation | Bajorek, M.,Schubert, H.L.,McCullough, J.,Langelier, C.,Eckert, D.M.,Stubblefield, W.M.,Uter, N.T.,Myszka, D.G.,Hill, C.P.,Sundquist, W.I. Structural basis for ESCRT-III protein autoinhibition. Nat.Struct.Mol.Biol., 16:754-762, 2009 Cited by PubMed Abstract: Endosomal sorting complexes required for transport-III (ESCRT-III) subunits cycle between two states: soluble monomers and higher-order assemblies that bind and remodel membranes during endosomal vesicle formation, midbody abscission and enveloped virus budding. Here we show that the N-terminal core domains of increased sodium tolerance-1 (IST1) and charged multivesicular body protein-3 (CHMP3) form equivalent four-helix bundles, revealing that IST1 is a previously unrecognized ESCRT-III family member. IST1 and its ESCRT-III binding partner, CHMP1B, both form higher-order helical structures in vitro, and IST1-CHMP1 interactions are required for abscission. The IST1 and CHMP3 structures also reveal that equivalent downstream alpha5 helices can fold back against the core domains. Mutations within the CHMP3 core-alpha5 interface stimulate the protein's in vitro assembly and HIV-inhibition activities, indicating that dissociation of the autoinhibitory alpha5 helix from the core activates ESCRT-III proteins for assembly at membranes. PubMed: 19525971DOI: 10.1038/nsmb.1621 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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