Summary for 8RVE
| Entry DOI | 10.2210/pdb8rve/pdb |
| EMDB information | 16844 |
| Descriptor | Vimentin (1 entity in total) |
| Functional Keywords | vimentin, intermediate filament, cytoskeleton, structural protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 78 |
| Total formula weight | 4190361.40 |
| Authors | Eibauer, M.,Medalia, O. (deposition date: 2024-02-01, release date: 2024-04-10, Last modification date: 2024-11-06) |
| Primary citation | Eibauer, M.,Weber, M.S.,Kronenberg-Tenga, R.,Beales, C.T.,Boujemaa-Paterski, R.,Turgay, Y.,Sivagurunathan, S.,Kraxner, J.,Koster, S.,Goldman, R.D.,Medalia, O. Vimentin filaments integrate low-complexity domains in a complex helical structure. Nat.Struct.Mol.Biol., 31:939-949, 2024 Cited by PubMed Abstract: Intermediate filaments (IFs) are integral components of the cytoskeleton. They provide cells with tissue-specific mechanical properties and are involved in numerous cellular processes. Due to their intricate architecture, a 3D structure of IFs has remained elusive. Here we use cryo-focused ion-beam milling, cryo-electron microscopy and tomography to obtain a 3D structure of vimentin IFs (VIFs). VIFs assemble into a modular, intertwined and flexible helical structure of 40 α-helices in cross-section, organized into five protofibrils. Surprisingly, the intrinsically disordered head domains form a fiber in the lumen of VIFs, while the intrinsically disordered tails form lateral connections between the protofibrils. Our findings demonstrate how protein domains of low sequence complexity can complement well-folded protein domains to construct a biopolymer with striking mechanical strength and stretchability. PubMed: 38632361DOI: 10.1038/s41594-024-01261-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.2 Å) |
Structure validation
Download full validation report
