9Z5N
Cryo-EM structure of rabbit vault cap
Summary for 9Z5N
| Entry DOI | 10.2210/pdb9z5n/pdb |
| EMDB information | 73819 |
| Descriptor | Major vault protein (1 entity in total) |
| Functional Keywords | complex, mvp, vault cap, trafficking, structural protein |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Total number of polymer chains | 39 |
| Total formula weight | 577160.14 |
| Authors | Li, H.,Clarke, O.B. (deposition date: 2025-11-12, release date: 2026-01-21, Last modification date: 2026-08-05) |
| Primary citation | Li, H.,Vallese, F.,Clarke, O.B. The vault particle is enclosed by a C 13-symmetric cap with a positively charged exterior. Sci Adv, 12:eadz6794-eadz6794, 2026 Cited by PubMed Abstract: Vaults are some of the largest ribonucleoprotein complexes known and are highly conserved across eukaryotes, but both their function and key details of their architecture remain unclear. While high-resolution structures of the vault shell are available, the architecture and symmetry of the cap have remained unresolved. Here, we present a 2.25-angstrom cryo-electron microscopy structure of the vault cap, revealing an unexpected 13-fold symmetric arrangement that contrasts with the 39-fold symmetry of the vault body, with each repeating module of the cap formed by an asymmetric homotrimer of adjacent subunits. The center of the cap features an unusual architecture, consisting of two concentric β barrels surrounded by an interwoven two-layer stack of α helices. The vault cap features a positively charged exterior and a negatively charged interior surface, with implications for binding partner recruitment and engineering of modified vault particles. PubMed: 41706843DOI: 10.1126/sciadv.adz6794 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.25 Å) |
Structure validation
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