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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | C15 symmetrized DEV collar | |||||||||
![]() | C15 symmetrized DEV collar | |||||||||
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![]() | complex / STRUCTURAL PROTEIN / gp53 | |||||||||
Function / homology | : / SGNH hydrolase-type esterase domain / GDSL-like Lipase/Acylhydrolase family / SGNH hydrolase superfamily / phosphatidylcholine lysophospholipase activity / SGNH hydrolase-type esterase domain-containing protein![]() | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.7 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 | ![]() | 16.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.6 KB 17.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 18.2 KB | Display | ![]() |
Images | ![]() | 29.1 KB | ||
Masks | ![]() | 512 MB | ![]() | |
Filedesc metadata | ![]() | 6.2 KB | ||
Others | ![]() ![]() | 410.4 MB 409.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9codMC ![]() 8vxqC ![]() 9bgmC ![]() 9bgnC ![]() 9bgoC 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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Annotation | C15 symmetrized DEV collar | ||||||||||||||||||||||||||||||||||||
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: Half Map A
File | emd_45776_half_map_1.map | ||||||||||||
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Annotation | Half Map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half Map B
File | emd_45776_half_map_2.map | ||||||||||||
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Annotation | Half Map B | ||||||||||||
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: SGNH hydrolase-type esterase domain-containing protein
Macromolecule | Name: SGNH hydrolase-type esterase domain-containing protein type: protein_or_peptide / ID: 1 / Number of copies: 15 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 118.10918 KDa |
Sequence | String: MTTKVIFTFH NPDGSPQANE KFTVRLTRPG MSDAEHCVVI PETYEMVTDA KGEFTMDLES STSAYRVTAI GDDDEYEDDP CSQYTFTFY VPDSADPVYV QELILMPPPT NLPWDEEAMN KITQAVVDAR EARDEAEAQA DRAEVQVDLA KAEVVKAQDE V VKAKAEVT ...String: MTTKVIFTFH NPDGSPQANE KFTVRLTRPG MSDAEHCVVI PETYEMVTDA KGEFTMDLES STSAYRVTAI GDDDEYEDDP CSQYTFTFY VPDSADPVYV QELILMPPPT NLPWDEEAMN KITQAVVDAR EARDEAEAQA DRAEVQVDLA KAEVVKAQDE V VKAKAEVT KAQAEVTKAA QQVELAKVEV GKAEASAAAA KVSETNAANA AAGSAASATA ATNQANRAKT EADRSKSEAD RA RDLADAM AEKVEGGSLP PLVGMNETFT YEGTDPYRWT VSGPATAVSD GSVMRLTKTD GSGSRAFVRQ AVSFPDSHWI VYM RVKTQT GTAAQNRSAQ IRFIAADKKD CVVYFNINAN GLVEPNTIHM QGTEGGTRNA ATMFTGLSTE TWLDLAVKYD AVNR HIELF RRLDTGVWQK GGGRLMVDAI KPAFIEVSSM PVAPQNWWLD LDFISVCKPN LICYGDSIAA GQNEYGVTRG SNSYN NNRN WAGTWFGKVP LYATNRNNLV LVQGVEGRRT WQYLSQLSEI SNSGVKVVFM HASTNDVNDA SMTMEKRTSD TQAIID QLH AVGAQVVLFN SMQGTKAYND ASSTTVKLRD YTDQWWNTEL PKVNGLAQTL DIARLIAKDG YMDPALGASD GLHLTNA SA QKIADKLGQF FSNSSDTNGF ASLDSPAFTG IPTVPTQTPF LPFGKTIANT EYVVTFIQDW TQRYGYGDLT MYSRTGAQ L SGGGVRSGYY HVPAGAGNPL PSGLNTSLAF VDHKSYDTNK GWQLWNPAYT GRLFIRTTNS AGTWQTPVEL ATFTWLDDN NVTKPRTLKF MELPLFNPPG SPSLSGFVPI QDSADGGWRN LSATPTGVAL LSASSAGGAL SYLGGMPIAN HTLPSNSIDN AALNGFYSV PSGTAGLPLG MDTTNGHAGI TSVFDNVTKY QLLFPRTGGA GSYATSVFYR ARSNNGWESW VRLLASNQLE G SVTTEPLT TAIFQNNGNN NQNVGRSVRF ADGTQIVYAT IRLTYSAVDV LQYTYTYPMG FVAPPTITVQ PILGARADIN DM PYFAVTS PFTYNVGNGN ALVQIYRVAG YTAHSFASTS FINCAVVAVG RWK UniProtKB: SGNH hydrolase-type esterase domain-containing 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 |