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- EMDB-4449: Localized reconstruction of tailknob of native bacteriophage P68 -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-4449 | ||||||||||||
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Title | Localized reconstruction of tailknob of native bacteriophage P68 | ||||||||||||
![]() | Localized reconstruction of a tailknob of native bacteriophage P68 | ||||||||||||
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Biological species | ![]() ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 11.3 Å | ||||||||||||
![]() | Hrebik D / Fuzik T / Skubnik K / Plevka P | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure and genome ejection mechanism of phage P68. Authors: Dominik Hrebík / Dana Štveráková / Karel Škubník / Tibor Füzik / Roman Pantůček / Pavel Plevka / ![]() Abstract: Phages infecting can be used as therapeutics against antibiotic-resistant bacterial infections. However, there is limited information about the mechanism of genome delivery of phages that infect ...Phages infecting can be used as therapeutics against antibiotic-resistant bacterial infections. However, there is limited information about the mechanism of genome delivery of phages that infect Gram-positive bacteria. Here, we present the structures of native phage P68, genome ejection intermediate, and empty particle. The P68 head contains 72 subunits of inner core protein, 15 of which bind to and alter the structure of adjacent major capsid proteins and thus specify attachment sites for head fibers. Unlike in the previously studied phages, the head fibers of P68 enable its virion to position itself at the cell surface for genome delivery. The unique interaction of one end of P68 DNA with one of the 12 portal protein subunits is disrupted before the genome ejection. The inner core proteins are released together with the DNA and enable the translocation of phage genome across the bacterial membrane into the cytoplasm. | ||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 5.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15 KB 15 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 4.7 KB | Display | ![]() |
Images | ![]() | 77.8 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 237.9 KB | Display | ![]() |
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Full document | ![]() | 237 KB | Display | |
Data in XML | ![]() | 8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4435C ![]() 4436C ![]() 4437C ![]() 4438C ![]() 4440C ![]() 4442C ![]() 4450C ![]() 4451C ![]() 4453C ![]() 4454C ![]() 4455C ![]() 4456C ![]() 4457C ![]() 4458C ![]() 4459C ![]() 6iabC ![]() 6iacC ![]() 6iatC ![]() 6iawC ![]() 6ib1C ![]() 6q3gC C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Localized reconstruction of a tailknob of native bacteriophage P68 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 2.126 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Staphylococcus phage P68
Entire | Name: ![]() ![]() |
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Components |
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-Supramolecule #1: Staphylococcus phage P68
Supramolecule | Name: Staphylococcus phage P68 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 204090 / Sci species name: Staphylococcus phage P68 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 6.9 KDa |
Virus shell | Shell ID: 1 / Name: Capsid / Diameter: 480.0 Å / T number (triangulation number): 4 |
-Macromolecule #1: Tailknob of bacteriophage P68
Macromolecule | Name: Tailknob of bacteriophage P68 / type: protein_or_peptide / ID: 1 / Enantiomer: DEXTRO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MRKLTNFKFF YNTPFTDYQN TIHFNSNKER DDYFLNGRHF KSLDYSKQPY NFIRDRMEIN VDMQWHDAQG INYMTFLSD FEDRRYYAFV NQIEYVNDVV VKIYFVIDTI MTYTQGNVLE QLSNVNIERQ HLSKRTYNYM L PMLRNNDD VLKVSNKNYV YNQMQQYLEN ...String: MRKLTNFKFF YNTPFTDYQN TIHFNSNKER DDYFLNGRHF KSLDYSKQPY NFIRDRMEIN VDMQWHDAQG INYMTFLSD FEDRRYYAFV NQIEYVNDVV VKIYFVIDTI MTYTQGNVLE QLSNVNIERQ HLSKRTYNYM L PMLRNNDD VLKVSNKNYV YNQMQQYLEN LVLFQSSADL SKKFGTKKEP NLDTSKGTIY DNITSPVNLY VM EYGDFIN FMDKMSAYPW ITQNFQKVQM LPKDFINTKD LEDVKTSEKI TGLKTLKQGG KSKEWSLKDL SLS FSKLQE MMLSKKDEFK HMIRNEYMTI EFYDWNGNTM LLDAGKISQK TGVKLRTKSI IGYHNEVRVY PVDY NSAEN DRPILAKNKE ILIDTGSFLN TNITFNSFAQ VPILINNGIL GQSQQANRQK NAESQLITNR IDNVL NGSD PKSRFYDAVS VASNLSPTAL FGKFNEEYNF YKQQQAEYKD LALQPPSVTE SEMGNAFQIA NSINGL TMK ISVPSPKEIT FLQKYYMLFG FEVNDYNSFI EPINSMTVCN YLKCTGTYTI RDIDPMLMEQ LKAILES GV RFWHNDGSGN PMLQNPLNNK FREGV |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 2 mg/mL | ||||||||||||
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Buffer | pH: 8 Component:
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Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: NITROGEN | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293 K / Instrument: FEI VITROBOT MARK IV / Details: blot time 2s; blot force -2; 3.6 ul of sample. |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Detector mode: INTEGRATING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Digitization - Frames/image: 1-7 / Number grids imaged: 2 / Number real images: 2891 / Average exposure time: 1.0 sec. / Average electron dose: 21.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 0.003 µm / Nominal defocus min: 0.001 µm / Nominal magnification: 75000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |