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Open data
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Basic information
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Title | Bacteriophage Sf14 Capsid Icosahedral reconstruction | |||||||||
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![]() | Sf14 / VIRUS | |||||||||
Function / homology | ![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
![]() | Subramanian S / Kerns HR / Braverman SG / Doore SM | |||||||||
Funding support | ![]()
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![]() | ![]() Title: The structure of Shigella virus Sf14 reveals the presence of two decoration proteins and two long tail fibers. Authors: Sundharraman Subramanian / Hailey R Kerns / Samantha G Braverman / Sarah M Doore / ![]() Abstract: Bacteriophage Sf14 infects the human pathogen Shigella flexneri. A previous low-resolution structure suggested the presence of a decoration protein on its T = 9 icosahedral capsid. Here, we ...Bacteriophage Sf14 infects the human pathogen Shigella flexneri. A previous low-resolution structure suggested the presence of a decoration protein on its T = 9 icosahedral capsid. Here, we determined high-resolution structures of the Sf14 capsid and neck, along with a moderate-resolution structure of the whole Sf14 tail and baseplate. These structures indicate the capsid has not one, but two different types of decoration proteins: a trimeric β-tulip lattice that covers the entire capsid and a set of Hoc-like proteins that bind preferentially to hexamers at the quasi-3-fold axes of symmetry. The neck also contains two sets of whiskers oriented in opposite directions, and the tail has two types of long tail fibers which may bind different receptors. Based on homology and phylogenetic analysis, Sf14 may be the product of multiple horizontal gene transfer events. The structures presented here can be used to investigate further hypotheses of phage structure-function relationships and structural diversity. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 3.5 GB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.4 KB 20.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 32.9 KB | Display | ![]() |
Images | ![]() | 254.5 KB | ||
Masks | ![]() | 3.7 GB | ![]() | |
Filedesc metadata | ![]() | 6.3 KB | ||
Others | ![]() ![]() | 3.4 GB 3.4 GB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 42.2 KB | Display | |
Data in CIF | ![]() | 58.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9c2dMC ![]() 9c39C ![]() 9c3aC ![]() 9c3bC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.224 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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-Half map: #1
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Density Histograms |
-Half map: #2
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Density Histograms |
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Sample components
-Entire : Shigella phage Sf14
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Shigella phage Sf14
Supramolecule | Name: Shigella phage Sf14 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 2024304 / Sci species name: Shigella phage Sf14 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() |
-Macromolecule #1: Major capsid protein
Macromolecule | Name: Major capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 9 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 41.595992 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MLTNSEKSRF FLADLTGEVQ SIPNTYGYIS GLGLFRSAPQ TQTTFLMDLT DWDISLLDAV DRTSRKAETS APERVRQISF PMMYFKEVE SITPDEIQGV RQPGTANELT TEAVVRAKKL MKIRTKFDIT REFLFMQALK GKVIDANGVL YADLYKQFDV T KKTIYFDL ...String: MLTNSEKSRF FLADLTGEVQ SIPNTYGYIS GLGLFRSAPQ TQTTFLMDLT DWDISLLDAV DRTSRKAETS APERVRQISF PMMYFKEVE SITPDEIQGV RQPGTANELT TEAVVRAKKL MKIRTKFDIT REFLFMQALK GKVIDANGVL YADLYKQFDV T KKTIYFDL DNPNSDIDAH IEDLRMHMED EAKTGTVING EEIHIVVDRT FFSKLIKHPK IRDAYLAQQT PLAWQQITGS LR TGGTDGV QAHMNRFYYG GVVFVQYNGK FKDKRGKTHT LVSIDGVSDT NVGVGHAFPN VAMLGEANNI FEVAYAPCPK MGY ANTLGQ ELYVFEYEKD RDEGIDFEAH SYMLPYCTRP QLLVDVRSDA E UniProtKB: Major capsid protein |
-Macromolecule #2: Structural protein
Macromolecule | Name: Structural protein / type: protein_or_peptide / ID: 2 / Number of copies: 9 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 13.574381 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MAYQGFTKLG EREPLNDIIL WEEITPTGHS RKEYAPVAST EYRVGEVLKA DGSKVAAGQE AQADSVCIVN FYADLQLSYH GQLKVVGIY RDAELKDLLK LESGVDAAAV KSALKAKGID FVPTGL UniProtKB: Putative structural protein |
-Macromolecule #3: Tail protein
Macromolecule | Name: Tail protein / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 39.336539 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MIKAKTYPDF KEFVKDFVAN VKAGKRYDFR KYQEAVLPLT YSSPWPESDI PEVTDFNYTP DYTVPFSEEL LYSVGAQMRT ADFFMDLQY AIINGKDVDT VYCEWLARVK PFSMLNAKLK DSAQPPVITT QPTGGAVNEG SAINLSIVAT NATSYQWKKG S SDISGATS ...String: MIKAKTYPDF KEFVKDFVAN VKAGKRYDFR KYQEAVLPLT YSSPWPESDI PEVTDFNYTP DYTVPFSEEL LYSVGAQMRT ADFFMDLQY AIINGKDVDT VYCEWLARVK PFSMLNAKLK DSAQPPVITT QPTGGAVNEG SAINLSIVAT NATSYQWKKG S SDISGATS ATYTKAGAVP ADAGSYTCVV TNDVGSTTSD AAVITINPLP VITTQPTSKA VNESSTLTLS VVATGATSYQ WK KNGTNIS GATSATYSKA NAKTTDAGSY TCVVTNAVGS VTSNAATVTI NPLPVITVQP QDQDLTVGQT LTISITATGA TGY QWRKGN SNISGATSAT YTKASVTTAD DGNYDCVVTN AVGSVTSHQA KVQVTA UniProtKB: Putative 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: 7.5 Component:
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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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: 33.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |