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- EMDB-44519: Pseudomonas phage DEV gp72 ejection protein (pre-ejection conform... -
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Open data
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Basic information
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Title | Pseudomonas phage DEV gp72 ejection protein (pre-ejection conformation) | |||||||||
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![]() | virion scaffolding / complex / STRUCTURAL PROTEIN / gp72 / ejection protein | |||||||||
Function / homology | Uncharacterized protein![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.2 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 | ![]() | 397.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.1 KB 14.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 18.1 KB | Display | ![]() |
Images | ![]() | 45.9 KB | ||
Masks | ![]() | 512 MB | ![]() | |
Filedesc metadata | ![]() | 5.5 KB | ||
Others | ![]() ![]() | 402.3 MB 403.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9bgoMC ![]() 8vxqC ![]() 9bgmC ![]() 9bgnC ![]() 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: #2
File | emd_44519_half_map_1.map | ||||||||||||
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Density Histograms |
-Half map: #1
File | emd_44519_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Scaffolding protein of Pseudomonas phage DEV
Entire | Name: Scaffolding protein of Pseudomonas phage DEV |
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Components |
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-Supramolecule #1: Scaffolding protein of Pseudomonas phage DEV
Supramolecule | Name: Scaffolding protein of Pseudomonas phage DEV / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: gp72
Macromolecule | Name: gp72 / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 57.183238 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MAQEITWRNI GATVSPGSAS SMSAGTTGVQ QALGALGDII SRQQEMNVNN AKLQREANTQ SYLDQVAAST LEQLSNADYR SGLEAQRDA MGMNLDRAAT RDAITKQISA QQNQAAATQK FDDMQAEVGQ RGIVDQLRTL SAEGRAGEVN QILAEQQLIN E GEIRKELT ...String: MAQEITWRNI GATVSPGSAS SMSAGTTGVQ QALGALGDII SRQQEMNVNN AKLQREANTQ SYLDQVAAST LEQLSNADYR SGLEAQRDA MGMNLDRAAT RDAITKQISA QQNQAAATQK FDDMQAEVGQ RGIVDQLRTL SAEGRAGEVN QILAEQQLIN E GEIRKELT GVQDAIQNRQ YRAAGEQRAQ AAANRAAEAH SLSMAAGREN LAFTREQRDE LRRDRDEAKL VSGTIATTFQ DY DESRQAQ SEIMRIVGKE VGMPTDDQGM PDMSRASQDQ LDAFSNALNE AGVQANTSPT ERRNAVLKSL VDAGVSSKGI AQA KQEMEL RESLEGLAPQ DRTKVEATIG AVNAELDTLQ RTATEDYERE VARNPFVEPD KDPLGSVNKI VDKAVKSGFG WEGD RQDLN NMLVDFATNG IKLPDGRTAV VPSKLLEQAF NTTNTWLFKN AGDVEKRIIE LMTTDGMTQM REDAPTIREN FLKTV SDIA NQKRSNAVKV TRSAEREKGV TMDPTDDLTF ALRGRKR UniProtKB: Uncharacterized 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 |