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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Cryo-EM structure of rabbit major vault protein complex | |||||||||
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Keywords | complex / MVP / vault cap / trafficking / STRUCTURAL PROTEIN | |||||||||
| 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 | single particle reconstruction / cryo EM / negative staining / Resolution: 2.4 Å | |||||||||
Authors | Li H / Clarke OB | |||||||||
| Funding support | 1 items
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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
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Downloads & links
-EMDB archive
| Map data | emd_73814.map.gz | 440.9 MB | EMDB map data format | |
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| Header (meta data) | emd-73814-v30.xml emd-73814.xml | 14.7 KB 14.7 KB | Display Display | EMDB header |
| Images | emd_73814.png | 80.1 KB | ||
| Filedesc metadata | emd-73814.cif.gz | 5.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-73814 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-73814 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9z4wMC ![]() 9z5nC ![]() 73813 C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_73814.map.gz / Format: CCP4 / Size: 1.3 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.105 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Major vault protein complex
| Entire | Name: Major vault protein complex |
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| Components |
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-Supramolecule #1: Major vault protein complex
| Supramolecule | Name: Major vault protein complex / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Major vault protein
| Macromolecule | Name: Major vault protein / type: protein_or_peptide / ID: 1 / Number of copies: 78 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 98.695156 KDa |
| Sequence | String: MATEESIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERILFDPVRM VTVPLRHYCV VANPVVRDAQ GSVVLDVTGQ VRLRHADME IRLTQDPFPL YPGELMEKGI TPLEVVLPNT ALHLRALLDF EDSNGEKVVA GDEWLFEGPG TYIPQKEVEV L QIIHATII ...String: MATEESIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERILFDPVRM VTVPLRHYCV VANPVVRDAQ GSVVLDVTGQ VRLRHADME IRLTQDPFPL YPGELMEKGI TPLEVVLPNT ALHLRALLDF EDSNGEKVVA GDEWLFEGPG TYIPQKEVEV L QIIHATII RPNEALRLRA RKEFCDRDGK QRVTGEEWLV RSVGAYLPGV FEEVLDLVGA VILTEKTALH LRARRNFQDV RG VTRRTGE EWLVTVQDTE AHVPDVHEEV LGVVPITTLG PQNYCVILDP VGPDGKNQLG QKRVVKGEKS FFLQPGESLE QGI QDVYVL SEQQGLLLRA LQPLEEGEGD ERVSHQAGDR WLIRGPLEYV PPVKVEVVEE RQAIPLDENE GIYVQDVKTG KVRA VIGST YMLTQDEILW DKELPPGVEE LLNKGHDPLA DRGEKVMAKP RQPPGPRNKT RVVSYRVPHN AAVQVYDYRE KKARV VFGP ELVSLGPEEQ FTVLSLSAGR PKRPHARRAL CLLLGPDFFT DVITIETADH ARLQLQLAYN WHFEVSDQRD PQETAK LFS VPDFVGDACK AIASRVRGAV ASVTFDDFHK NSARIIRAAV FGFETAEAKG PDGMALPRPR DRAVFPQNGL VVSSVDV QS VEPVDQRTRD ALQRSVQLAI EITTNSQEAA AKHEAQRLEQ EARGRLERQK ILDQSEAEKA RKELLELEAL SMAVESTG T AKAEAESRAE AARIEGEGSV LQAKLKAQAL AIETEAELQR VQKVRELELV YARAQLELEV SKAQQLAEVE AKKFKQMTE ALGPSTIKDL AVAGPEMQVK LLQSLGLKST LITDGSTPVN LFNTAFGLLG LGADGQPLGR MTAGGPRLQE AASPQSPSAP LAPGSTHIL P UniProtKB: Major vault protein |
-Experimental details
-Structure determination
| Method | negative staining, cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | tissue |
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Sample preparation
| Buffer | pH: 6.8 |
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| Staining | Type: NEGATIVE / Material: Uranyl Acetate |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 34.4 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: DIFFRACTION / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Processing
FIELD EMISSION GUN

