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Open data
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Basic information
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| Title | Portal protein of full Haloferax tailed virus 1. | |||||||||
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Sample |
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Keywords | Archaeal virus / portal / portal capsid interface / Mg ions / VIRUS | |||||||||
| Function / homology | Portal protein / HK97 gp6-like/SPP1 gp15-like head-tail connector Function and homology information | |||||||||
| Biological species | Haloferax tailed virus 1 | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.342 Å | |||||||||
Authors | Zhang D / Daum B / Isupov MN / McLaren M | |||||||||
| Funding support | European Union, 1 items
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Citation | Journal: Sci Adv / Year: 2025Title: Cryo-EM resolves the structure of the archaeal dsDNA virus HFTV1 from head to tail. Authors: Daniel X Zhang / Michail N Isupov / Rebecca M Davies / Sabine Schwarzer / Mathew McLaren / William S Stuart / Vicki A M Gold / Hanna M Oksanen / Tessa E F Quax / Bertram Daum / ![]() Abstract: While archaeal viruses show a stunning diversity of morphologies, many bear a notable resemblance to tailed bacterial phages. This raises fundamental questions: Do all tailed viruses share a common ...While archaeal viruses show a stunning diversity of morphologies, many bear a notable resemblance to tailed bacterial phages. This raises fundamental questions: Do all tailed viruses share a common origin and do they infect their hosts in similar ways? Answering these questions requires high-resolution structural insights, yet no complete atomic models of archaeal viruses have been available. Here, we present the near-atomic resolution structure of Haloferax tailed virus 1 (HFTV1), an archaeal virus thriving in extreme salinity. Using cryo-electron microscopy, we resolve the architecture and assembly of all structural proteins and capture conformational transitions associated with DNA ejection. Our data reveal genome spooling within the capsid and identify putative receptor-binding and catalytic sites for host recognition and infection. These findings uncover key mechanisms of archaeal virus assembly, principles of virus-host interactions, and evolutionary links connecting archaeal, bacterial, and eukaryotic viruses. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_18599.map.gz | 123.2 MB | EMDB map data format | |
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| Header (meta data) | emd-18599-v30.xml emd-18599.xml | 21.2 KB 21.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_18599_fsc.xml | 12.4 KB | Display | FSC data file |
| Images | emd_18599.png | 94.8 KB | ||
| Filedesc metadata | emd-18599.cif.gz | 6.5 KB | ||
| Others | emd_18599_additional_1.map.gz emd_18599_half_map_1.map.gz emd_18599_half_map_2.map.gz | 191 MB 123.4 MB 124.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-18599 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-18599 | HTTPS FTP |
-Validation report
| Summary document | emd_18599_validation.pdf.gz | 832.2 KB | Display | EMDB validaton report |
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| Full document | emd_18599_full_validation.pdf.gz | 831.8 KB | Display | |
| Data in XML | emd_18599_validation.xml.gz | 19.8 KB | Display | |
| Data in CIF | emd_18599_validation.cif.gz | 26.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18599 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18599 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8qqnMC ![]() 8qpgC ![]() 8qpqC ![]() 8qsiC ![]() 8qsyC ![]() 9fkbC ![]() 9gs0C ![]() 9h4pC ![]() 9h5bC ![]() 9h7vC M: atomic model generated by this map C: citing same article ( |
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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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Map
| File | Download / File: emd_18599.map.gz / Format: CCP4 / Size: 166.4 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: 1.171 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: EMReady map
| File | emd_18599_additional_1.map | ||||||||||||
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| Annotation | EMReady map | ||||||||||||
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-Half map: #2
| File | emd_18599_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_18599_half_map_2.map | ||||||||||||
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Sample components
-Entire : Haloferax tailed virus 1
| Entire | Name: Haloferax tailed virus 1 |
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| Components |
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-Supramolecule #1: Haloferax tailed virus 1
| Supramolecule | Name: Haloferax tailed virus 1 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 / NCBI-ID: 2507575 / Sci species name: Haloferax tailed virus 1 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No |
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| Host (natural) | Organism: Haloferax gibbonsii (archaea) |
-Macromolecule #1: HK97 gp6-like/SPP1 gp15-like head-tail connector
| Macromolecule | Name: HK97 gp6-like/SPP1 gp15-like head-tail connector / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
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| Source (natural) | Organism: Haloferax tailed virus 1 |
| Molecular weight | Theoretical: 15.585868 KDa |
| Sequence | String: MPDPSIDEVS KSDWDALTTQ EQDDIISQVE NLSSTGWVNT SRERKAEAIR SAIAERDTLY SGNMSRLPTL DGDAEYFTLY LSAHKIQLF EGGEAQSESG EGGSVSYSTG GGGEKDLQKT RYGRMALEYV WEDNSIAALR TY UniProtKB: HK97 gp6-like/SPP1 gp15-like head-tail connector |
-Macromolecule #2: Portal protein
| Macromolecule | Name: Portal protein / type: protein_or_peptide / ID: 2 / Number of copies: 12 / Enantiomer: LEVO |
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| Source (natural) | Organism: Haloferax tailed virus 1 |
| Molecular weight | Theoretical: 75.680906 KDa |
| Sequence | String: MPKYNLRIGN RRVPIASTDT PLSEAIGKRL ASSTPQTNVD SMGGGHSYQF NGQDLTFEDL RDIKDVRDSG GQVAQLMDYK ALLNFGEGC EIHVEGDDET KQLVDGEPMT LSEWLEDAFP HLDLLVLDLG GDALWYPYAV GEIQETITGE FKEALPAEPW T LMPESDAQ ...String: MPKYNLRIGN RRVPIASTDT PLSEAIGKRL ASSTPQTNVD SMGGGHSYQF NGQDLTFEDL RDIKDVRDSG GQVAQLMDYK ALLNFGEGC EIHVEGDDET KQLVDGEPMT LSEWLEDAFP HLDLLVLDLG GDALWYPYAV GEIQETITGE FKEALPAEPW T LMPESDAQ GKVQAWHQRT KTHGGYQTQT LPADDLW(HIP)IV INKASARDEV GISEVLRNKD EIQAFKQNEA AINQAIEL H GFPQR(HIP)VKVG KEDGAPVRDN DLRRVRTIFD PRTTDANTAY FTGQDVDVET LEA(HIP)NFDYSA IHEMDMRNLT T ALGLPLEA GNVGADGLGS GKPAELRFAL LKLAIKANQR SFSVQFVERV MRPVVRDYSP FDHEADIRLE INDPLEDIGE VA DLIQQVG DYMTNEQVAE KLDLPAPEDD EVADSYRSPA DMEKDEAGVQ DEPFGGMFAG RDMGNRCLGE GITDDELQHA PEW DRPLLE MYQGVTNPES DTSRTLVSFS SSGTPEFVLE RIRESIMDGA LFSEFDNIPS SRLMELRQTF ADELGTDNFT LDSI TDALM DFEADLTRDA AERIARTESS AVLNHAREIS YEERGEGNEL FYWTGADLGD SRQTEACAWL IRQTNPFSGG TPVPM NELR DMVDEAPSHD DSMDNNLARP DSWVVHPNER SSFVKAPPNW EQL UniProtKB: Portal protein |
-Macromolecule #3: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 12 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 Da |
-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 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | #0 - Image recording ID: 1 / #0 - Film or detector model: TFS FALCON 4i (4k x 4k) / #0 - Average electron dose: 50.0 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K3 (6k x 4k) / #1 - Average electron dose: 54.6 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Initial model type: in silico model |
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| Refinement | Space: RECIPROCAL / Protocol: AB INITIO MODEL |
| Output model | ![]() PDB-8qqn: |
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About Yorodumi




Haloferax tailed virus 1
Keywords
Authors
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Haloferax gibbonsii (archaea)
FIELD EMISSION GUN

