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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Pseudomonas phage DEV 5-fold vertex (major coat protein) | |||||||||
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![]() | virion coat / complex / STRUCTURAL PROTEIN / gp77 | |||||||||
Function / homology | Phage capsid protein / Major coat protein![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
![]() | Iglesias SM / Hou CFD / Li F / Cingolani G | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Integrative structural analysis of Pseudomonas phage DEV reveals a genome ejection motor. Authors: Ravi K Lokareddy / Chun-Feng David Hou / Francesca Forti / Stephano M Iglesias / Fenglin Li / Mikhail Pavlenok / David S Horner / Michael Niederweis / Federica Briani / Gino Cingolani / ![]() ![]() Abstract: DEV is an obligatory lytic Pseudomonas phage of the N4-like genus, recently reclassified as Schitoviridae. The DEV genome encodes 91 ORFs, including a 3398 amino acid virion-associated RNA polymerase ...DEV is an obligatory lytic Pseudomonas phage of the N4-like genus, recently reclassified as Schitoviridae. The DEV genome encodes 91 ORFs, including a 3398 amino acid virion-associated RNA polymerase (vRNAP). Here, we describe the complete architecture of DEV, determined using a combination of cryo-electron microscopy localized reconstruction, biochemical methods, and genetic knockouts. We built de novo structures of all capsid factors and tail components involved in host attachment. We demonstrate that DEV long tail fibers are essential for infection of Pseudomonas aeruginosa but dispensable for infecting mutants with a truncated lipopolysaccharide devoid of the O-antigen. We determine that DEV vRNAP is part of a three-gene operon conserved in 191 Schitoviridae genomes. We propose these three proteins are ejected into the host to form a genome ejection motor spanning the cell envelope. We posit that the design principles of the DEV ejection apparatus are conserved in all Schitoviridae. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 472.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.1 KB 14.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 18.1 KB | Display | ![]() |
Images | ![]() | 104.1 KB | ||
Masks | ![]() | 512 MB | ![]() | |
Filedesc metadata | ![]() | 5.5 KB | ||
Others | ![]() ![]() | 412.9 MB 411.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 26.3 KB | Display | |
Data in CIF | ![]() | 35.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9bgnMC ![]() 8vxqC ![]() 9bgmC ![]() 9bgoC ![]() 9codC 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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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.12 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: #1
File | emd_44518_half_map_1.map | ||||||||||||
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Density Histograms |
-Half map: #2
File | emd_44518_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Major coat protein of Pseudomonas phage DEV
Entire | Name: Major coat protein of Pseudomonas phage DEV |
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Components |
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-Supramolecule #1: Major coat protein of Pseudomonas phage DEV
Supramolecule | Name: Major coat protein of Pseudomonas phage DEV / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: gp77 major coat protein
Macromolecule | Name: gp77 major coat protein / type: protein_or_peptide / ID: 1 / Number of copies: 9 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 44.114113 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MAGPVDNIKP MKYNDPANGV ESSIGPQIHT RYWYKRALID AAKEAYFGQL ADTFSMPKHY GKEIVRLHYI PLLDDRNVND QGIDASGAT IANGNLYGSS RDVGNITAKM PTLTEIGGRV NRVGFKRVEI KGKLEKYGFF REYTQEQLDF DSDPAMEGHV T TEMVKGAN ...String: MAGPVDNIKP MKYNDPANGV ESSIGPQIHT RYWYKRALID AAKEAYFGQL ADTFSMPKHY GKEIVRLHYI PLLDDRNVND QGIDASGAT IANGNLYGSS RDVGNITAKM PTLTEIGGRV NRVGFKRVEI KGKLEKYGFF REYTQEQLDF DSDPAMEGHV T TEMVKGAN EITEDLLQID LLNSAGTVRY PGAATSDAEV DASTEVTYDS LMRLRLDLDN ARAPTKIKMI TGTRMIDTRT VG NARALYV GSDLVPTIEA MKDNHGNPAF IPIEKYAAGG ATMHGEVGQL GRFRVIVNPQ MMHWAGVGKA VDPNDQVPMH ESG GKYSVF PMLCVASEAF TTVGFATDGK NVKFKIITKR PGEATADRSD PYGEMGFMSI KWYYGFMVFR PEWIALLKTV ARL UniProtKB: Major coat 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 |
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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 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |