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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | SaPI1 neck structure | |||||||||
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![]() | sapi / capsid / tail / phage / VIRUS LIKE PARTICLE | |||||||||
Function / homology | Bacteriophage 69, Orf23, major tail protein / Phage gp6-like head-tail connector protein / Phage gp6-like head-tail connector protein / Phage major tail protein TP901-1 / Phage tail tube protein / Uncharacterized protein / DUF3168 domain-containing protein / Major tail protein / Head-tail connector protein![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.14 Å | |||||||||
![]() | Kizziah JL / Dokland T | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of the Staphylococcus aureus bacteriophage 80α neck shows details of the DNA, tail completion protein, and tape measure protein. Authors: James L Kizziah / Amarshi Mukherjee / Laura K Parker / Terje Dokland / ![]() Abstract: The Staphylococcus aureus pathogenicity islands (SaPIs), including SaPI1, are a type of mobile genetic elements (MGEs) that are mobilized at high frequency by "helper" bacteriophages, such as 80α, ...The Staphylococcus aureus pathogenicity islands (SaPIs), including SaPI1, are a type of mobile genetic elements (MGEs) that are mobilized at high frequency by "helper" bacteriophages, such as 80α, leading to packaging of the SaPI genomes into virions made from helper-encoded structural proteins. 80α and SaPI1 virions consist of an icosahedral head connected via a portal vertex to a long, non-contractile tail. A connector or "neck" forms the interface between the tail and the head. Here, we have determined the high-resolution structure of the neck section of SaPI1 virions, including the dodecameric portal and head-tail-connector proteins, and the hexameric head-tail joining, tail terminator and major tail proteins. We also resolved the DNA, the tail completion protein (TCP), and the tape measure protein (TMP) inside the tail, features that have not previously been observed at high resolution. Our study provides insights into the assembly and infection process in this important group of MGEs. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 49.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.5 KB 17.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 7.9 KB | Display | ![]() |
Images | ![]() | 104.5 KB | ||
Masks | ![]() | 52.7 MB | ![]() | |
Filedesc metadata | ![]() | 5.6 KB | ||
Others | ![]() ![]() | 48.5 MB 48.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9mu3MC ![]() 9mu2C C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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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
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Density Histograms |
-Half map: #2
File | emd_48618_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
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Density Histograms |
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Sample components
-Entire : Staphylococcus phage 80alpha
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Staphylococcus phage 80alpha
Supramolecule | Name: Staphylococcus phage 80alpha / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / Details: SaPI1 virion / NCBI-ID: 2911440 / Sci species name: Staphylococcus phage 80alpha / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No |
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-Macromolecule #1: Head-tail connector protein
Macromolecule | Name: Head-tail connector protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 12.809583 KDa |
Sequence | String: MTTLADVKKR IGLKDEKQDE QLEEIIKSCE SQLLSMLPIE VEQIPERFSY MIKEVAVKRY NRIGAEGMTS EAVDGRSNAY ELNDFKEYE AIIDNYFNAR TRTKKGRAVF F UniProtKB: Head-tail connector protein |
-Macromolecule #2: adaptor
Macromolecule | Name: adaptor / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 11.815448 KDa |
Sequence | String: MRYEDRVIFQ LEQVATYNPK TSKKENTLIT YDAIPCNINP ISRARKQLEF GDVKNDVSVL RIKESISYPV SHVLVNGIRY KIVDTRIYR HETSYYIEEV N UniProtKB: Uncharacterized protein |
-Macromolecule #3: DUF3168 domain-containing protein
Macromolecule | Name: DUF3168 domain-containing protein / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 14.730251 KDa |
Sequence | String: MTPNLQLYNK AYETLQGYGF PVISRKEMQQ EIPYPFFVIK MPESNRSKYT FDSYSGDTNL VIDIWSVSDD LGHHDGLVKR CIDDLTPSV KTNDYDFEED DTNITQLVDD TTNQELLHTS ITISYKTF UniProtKB: DUF3168 domain-containing protein |
-Macromolecule #4: Major tail protein
Macromolecule | Name: Major tail protein / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 21.551746 KDa |
Sequence | String: MANMKNSNDR IILFRKAGEK VDATKMLFLT EYGLSHEADT DTEDTMDGSY NTGGSVESTM SGTAKMFYGD DFADEIEDAV VDRVLYEAW EVESRIPGKN GDSAKFKAKY FQGFHNKFEL KAEANGIDEY EYEYGVNGRF QRGFATLPEA VTKKLKATGY R FHDTTKED ...String: MANMKNSNDR IILFRKAGEK VDATKMLFLT EYGLSHEADT DTEDTMDGSY NTGGSVESTM SGTAKMFYGD DFADEIEDAV VDRVLYEAW EVESRIPGKN GDSAKFKAKY FQGFHNKFEL KAEANGIDEY EYEYGVNGRF QRGFATLPEA VTKKLKATGY R FHDTTKED ALTSEDLTAI PQPKVDSSTV TPGEV UniProtKB: Major tail protein |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | 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 | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 35.26 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
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 |