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Open data
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Basic information
| Entry | ![]() | |||||||||||||||
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| Title | SaPI1 mature capsid structure containing DNA | |||||||||||||||
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Keywords | capsid / phage / sapi / VIRUS LIKE PARTICLE | |||||||||||||||
| Function / homology | : / Phage capsid / Phage capsid family / viral capsid / Major capsid protein Function and homology information | |||||||||||||||
| Biological species | Dubowvirus dv80alpha | |||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||||||||
Authors | Mukherjee A / Kizziah JL / Dokland T | |||||||||||||||
| Funding support | United States, 4 items
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Citation | Journal: J Mol Biol / Year: 2024Title: Structure of the Portal Complex from Staphylococcus aureus Pathogenicity Island 1 Transducing Particles In Situ and In Isolation. Authors: Amarshi Mukherjee / James L Kizziah / N'Toia C Hawkins / Mohamed O Nasef / Laura K Parker / Terje Dokland / ![]() Abstract: Staphylococcus aureus is an important human pathogen, and the prevalence of antibiotic resistance is a major public health concern. The evolution of pathogenicity and resistance in S. aureus often ...Staphylococcus aureus is an important human pathogen, and the prevalence of antibiotic resistance is a major public health concern. The evolution of pathogenicity and resistance in S. aureus often involves acquisition of mobile genetic elements (MGEs). Bacteriophages play an especially important role, since transduction represents the main mechanism for horizontal gene transfer. S. aureus pathogenicity islands (SaPIs), including SaPI1, are MGEs that carry genes encoding virulence factors, and are mobilized at high frequency through interactions with specific "helper" bacteriophages, such as 80α, leading to packaging of the SaPI genomes into virions made from structural proteins supplied by the helper. Among these structural proteins is the portal protein, which forms a ring-like portal at a fivefold vertex of the capsid, through which the DNA is packaged during virion assembly and ejected upon infection of the host. We have used high-resolution cryo-electron microscopy to determine structures of the S. aureus bacteriophage 80α portal itself, produced by overexpression, and in situ in the empty and full SaPI1 virions, and show how the portal interacts with the capsid. These structures provide a basis for understanding portal and capsid assembly and the conformational changes that occur upon DNA packaging and ejection. | |||||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_43142.map.gz | 123.5 MB | EMDB map data format | |
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| Header (meta data) | emd-43142-v30.xml emd-43142.xml | 15.4 KB 15.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_43142_fsc.xml | 26.9 KB | Display | FSC data file |
| Images | emd_43142.png | 90 KB | ||
| Masks | emd_43142_msk_1.map | 1.7 GB | Mask map | |
| Filedesc metadata | emd-43142.cif.gz | 5.5 KB | ||
| Others | emd_43142_half_map_1.map.gz emd_43142_half_map_2.map.gz | 1.3 GB 1.3 GB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-43142 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-43142 | HTTPS FTP |
-Validation report
| Summary document | emd_43142_validation.pdf.gz | 668.9 KB | Display | EMDB validaton report |
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| Full document | emd_43142_full_validation.pdf.gz | 668.5 KB | Display | |
| Data in XML | emd_43142_validation.xml.gz | 33.2 KB | Display | |
| Data in CIF | emd_43142_validation.cif.gz | 45.9 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-43142 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-43142 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8vd4MC ![]() 8v8bC ![]() 8vd5C ![]() 8vd8C ![]() 8vdcC ![]() 8vdeC 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_43142.map.gz / Format: CCP4 / Size: 1.7 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: 1.33 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_43142_msk_1.map | ||||||||||||
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-Half map: #1
| File | emd_43142_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_43142_half_map_2.map | ||||||||||||
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Sample components
-Entire : Dubowvirus dv80alpha
| Entire | Name: Dubowvirus dv80alpha |
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| Components |
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-Supramolecule #1: Dubowvirus dv80alpha
| Supramolecule | Name: Dubowvirus dv80alpha / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 53369 / Sci species name: Dubowvirus dv80alpha / Virus type: SATELLITE / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No |
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-Macromolecule #1: Major head protein
| Macromolecule | Name: Major head protein / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: Dubowvirus dv80alpha |
| Molecular weight | Theoretical: 36.846883 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MEQTQKLKLN LQHFASNNVK PQVFNPDNVM MHEKKDGTLM NEFTTPILQE VMENSKIMQL GKYEPMEGTE KKFTFWADKP GAYWVGEGQ KIETSKATWV NATMRAFKLG VILPVTKEFL NYTYSQFFEE MKPMIAEAFY KKFDEAGILN QGNNPFGKSI A QSIEKTNK ...String: MEQTQKLKLN LQHFASNNVK PQVFNPDNVM MHEKKDGTLM NEFTTPILQE VMENSKIMQL GKYEPMEGTE KKFTFWADKP GAYWVGEGQ KIETSKATWV NATMRAFKLG VILPVTKEFL NYTYSQFFEE MKPMIAEAFY KKFDEAGILN QGNNPFGKSI A QSIEKTNK VIKGDFTQDN IIDLEALLED DELEANAFIS KTQNRSLLRK IVDPETKERI YDRNSDSLDG LPVVNLKSSN LK RGELITG DFDKLIYGIP QLIEYKIDET AQLSTVKNED GTPVNLFEQD MVALRATMHV ALHIADDKAF AKLVPADKRT DSV PGEV UniProtKB: Major capsid protein |
-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: 7.8 |
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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: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 35.26 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: 0.7000000000000001 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Dubowvirus dv80alpha
Keywords
Authors
United States, 4 items
Citation












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Processing
FIELD EMISSION GUN

