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Open data
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Basic information
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| Title | The capsid structure of Aleutian Mink Disease Virus | |||||||||
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Keywords | Parvovirus / Capsid / AMDV / cryo-EM / Amdoparvovirus / Pathogen / VIRUS LIKE PARTICLE | |||||||||
| Function / homology | Function and homology informationsymbiont entry into host cell via permeabilization of host membrane / T=1 icosahedral viral capsid / clathrin-dependent endocytosis of virus by host cell / virion attachment to host cell / host cell nucleus / structural molecule activity Similarity search - Function | |||||||||
| Biological species | Aleutian mink disease virus | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.37 Å | |||||||||
Authors | Mietzsch M / McKenna R | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Viruses / Year: 2022Title: Capsid Structure of Aleutian Mink Disease Virus and Human Parvovirus 4: New Faces in the Parvovirus Family Portrait. Authors: Renuk Lakshmanan / Mario Mietzsch / Alberto Jimenez Ybargollin / Paul Chipman / Xiaofeng Fu / Jianming Qiu / Maria Söderlund-Venermo / Robert McKenna / ![]() Abstract: Parvoviruses are small, single-stranded DNA viruses with non-enveloped capsids. Determining the capsid structures provides a framework for annotating regions important to the viral life cycle. ...Parvoviruses are small, single-stranded DNA viruses with non-enveloped capsids. Determining the capsid structures provides a framework for annotating regions important to the viral life cycle. Aleutian mink disease virus (AMDV), a pathogen in minks, and human parvovirus 4 (PARV4), infecting humans, are parvoviruses belonging to the genera and , respectively. While Aleutian mink disease caused by AMDV is a major threat to mink farming, no clear clinical manifestations have been established following infection with PARV4 in humans. Here, the capsid structures of AMDV and PARV4 were determined via cryo-electron microscopy at 2.37 and 3.12 Å resolutions, respectively. Despite low amino acid sequence identities (10-30%) both viruses share the icosahedral nature of parvovirus capsids, with 60 viral proteins (VPs) assembling the capsid via two-, three-, and five-fold symmetry VP-related interactions, but display major structural variabilities in the surface loops when the capsid structures are superposed onto other parvoviruses. The capsid structures of AMDV and PARV4 will add to current knowledge of the structural platform for parvoviruses and permit future functional annotation of these viruses, which will help in understanding their infection mechanisms at a molecular level for the development of diagnostics and therapeutics. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_28514.map.gz | 443 MB | EMDB map data format | |
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| Header (meta data) | emd-28514-v30.xml emd-28514.xml | 16.7 KB 16.7 KB | Display Display | EMDB header |
| Images | emd_28514.png | 71.7 KB | ||
| Filedesc metadata | emd-28514.cif.gz | 6.1 KB | ||
| Others | emd_28514_half_map_1.map.gz emd_28514_half_map_2.map.gz | 147.6 MB 147.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-28514 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-28514 | HTTPS FTP |
-Validation report
| Summary document | emd_28514_validation.pdf.gz | 945.6 KB | Display | EMDB validaton report |
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| Full document | emd_28514_full_validation.pdf.gz | 945.2 KB | Display | |
| Data in XML | emd_28514_validation.xml.gz | 19.1 KB | Display | |
| Data in CIF | emd_28514_validation.cif.gz | 21.7 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28514 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28514 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8ep2MC ![]() 8ep9C 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_28514.map.gz / Format: CCP4 / Size: 476.8 MB / 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: 0.949 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_28514_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_28514_half_map_2.map | ||||||||||||
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Sample components
-Entire : Aleutian mink disease virus
| Entire | Name: Aleutian mink disease virus |
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| Components |
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-Supramolecule #1: Aleutian mink disease virus
| Supramolecule | Name: Aleutian mink disease virus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 28314 / Sci species name: Aleutian mink disease virus / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: Yes |
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| Virus shell | Shell ID: 1 / T number (triangulation number): 1 |
-Macromolecule #1: Capsid protein VP1
| Macromolecule | Name: Capsid protein VP1 / type: protein_or_peptide / ID: 1 / Number of copies: 60 / Enantiomer: LEVO |
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| Source (natural) | Organism: Aleutian mink disease virus |
| Molecular weight | Theoretical: 73.595305 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MDSTEAEQMD TEQATNQTAE AGGGGGGGGG GGGGGGGVGN STGGFNNTTE FKVINNEVYI TCHATRMVHI NQADTDEYLI FNAGRTTDT KTHQQKLNLE FFVYDDFHQQ VMTPWYIVDS NAWGVWMSPK DFQQMKTLCS EISLVTLEQE IDNVTIKTVT E TNQGNAST ...String: MDSTEAEQMD TEQATNQTAE AGGGGGGGGG GGGGGGGVGN STGGFNNTTE FKVINNEVYI TCHATRMVHI NQADTDEYLI FNAGRTTDT KTHQQKLNLE FFVYDDFHQQ VMTPWYIVDS NAWGVWMSPK DFQQMKTLCS EISLVTLEQE IDNVTIKTVT E TNQGNAST KQFNNDLTAS LQVALDTNNI LPYTPAAPLG ETLGFVPWRA TKPTQYRYYH PCYIYNRYPN IQKVATETLT WD AVQDDYL SVDEQYFNFI TIENNIPINI LRTGDNFHTG LYEFNSKPCK LTLSYQSTRC LGLPPLCKPK TDTTHKVTSK ENG ADLIYI QGQDNTRLGH FWGEERGKKN AEMNRIRPYN IGYQYPEWII PAGLQGSYFA GGPRQWSDTT KGAGTHSQHL QQNF STRYI YDRNHGGDNE VDLLDGIPIH ERSNYYSDNE IEQHTAKQPK LRTPPIHHSK IDSWEEEGWP AASGTHFEDE VIYLD YFNF SGEQELNFPH EVLDDAAQMK KLLNSYQPTV AQDNVGPVYP WGQIWDKKPH MDHKPSMNNN APFVCKNNPP GQLFVK LTE NLTDTFNYDE NPDRIKTYGY FTWRGKLVLK GKLSQVTCWN PVKRELIGEP GVFTKDKYHK QIPNNKGNFE IGLQYGR ST IKYIY UniProtKB: Capsid protein VP1 |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: DIRECT ELECTRON APOLLO (4k x 4k) / Average electron dose: 59.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Aleutian mink disease virus
Keywords
Authors
United States, 1 items
Citation







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Processing
FIELD EMISSION GUN
