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Open data
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Basic information
| Entry | Database: PDB / ID: 9z4w | |||||||||||||||
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| Title | Cryo-EM structure of rabbit major vault protein complex | |||||||||||||||
Components | Major vault protein | |||||||||||||||
Keywords | STRUCTURAL PROTEIN / complex / MVP / vault cap / trafficking | |||||||||||||||
| Function / homology | Function and homology informationprotein activation cascade / ERBB signaling pathway / negative regulation of epidermal growth factor receptor signaling pathway / cell population proliferation / protein phosphatase binding / cytoskeleton / ribonucleoprotein complex / protein kinase binding / perinuclear region of cytoplasm / identical protein binding ...protein activation cascade / ERBB signaling pathway / negative regulation of epidermal growth factor receptor signaling pathway / cell population proliferation / protein phosphatase binding / cytoskeleton / ribonucleoprotein complex / protein kinase binding / perinuclear region of cytoplasm / identical protein binding / nucleus / cytosol Similarity search - Function | |||||||||||||||
| Biological species | ![]() | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.4 Å | |||||||||||||||
Authors | Li, H. / Clarke, O.B. | |||||||||||||||
| Funding support | 1items
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Citation | Journal: Sci Adv / Year: 2026Title: The vault particle is enclosed by a 13-symmetric cap with a positively charged exterior. Authors: Huan Li / Francesca Vallese / Oliver B Clarke / ![]() 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- ...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. | |||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9z4w.cif.gz | 10.2 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9z4w.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9z4w.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z4/9z4w ftp://data.pdbj.org/pub/pdb/validation_reports/z4/9z4w | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 73814MC ![]() 9z5nC ![]() 73813 C: citing same article ( M: map data used to model this data |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| Noncrystallographic symmetry (NCS) | NCS oper:
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Components
| #1: Protein | Mass: 98695.156 Da / Num. of mol.: 78 / Source method: isolated from a natural source / Source: (natural) ![]() Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: TISSUE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Major vault protein complex / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: all / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 6.8 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| EM staining | Type: NEGATIVE / Material: Uranyl Acetate |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: DIFFRACTION / Nominal defocus max: 1500 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 34.4 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||
| 3D reconstruction | Resolution: 2.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 159668 / Symmetry type: POINT |
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FIELD EMISSION GUN