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Open data
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Basic information
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Title | Pseudomonas phage E217 contracted sheath | |||||||||
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Function / homology | Protein of unknown function DUF3383 / Protein of unknown function (DUF3383) / Tail sheath protein![]() | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Li F / Cingolani G / Hou C | |||||||||
Funding support | ![]()
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![]() | ![]() Title: High-resolution cryo-EM structure of the Pseudomonas bacteriophage E217. Authors: Fenglin Li / Chun-Feng David Hou / Ravi K Lokareddy / Ruoyu Yang / Francesca Forti / Federica Briani / Gino Cingolani / ![]() ![]() Abstract: E217 is a Pseudomonas phage used in an experimental cocktail to eradicate cystic fibrosis-associated Pseudomonas aeruginosa. Here, we describe the structure of the whole E217 virion before and after ...E217 is a Pseudomonas phage used in an experimental cocktail to eradicate cystic fibrosis-associated Pseudomonas aeruginosa. Here, we describe the structure of the whole E217 virion before and after DNA ejection at 3.1 Å and 4.5 Å resolution, respectively, determined using cryogenic electron microscopy (cryo-EM). We identify and build de novo structures for 19 unique E217 gene products, resolve the tail genome-ejection machine in both extended and contracted states, and decipher the complete architecture of the baseplate formed by 66 polypeptide chains. We also determine that E217 recognizes the host O-antigen as a receptor, and we resolve the N-terminal portion of the O-antigen-binding tail fiber. We propose that E217 design principles presented in this paper are conserved across PB1-like Myoviridae phages of the Pbunavirus genus that encode a ~1.4 MDa baseplate, dramatically smaller than the coliphage T4. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 79.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.2 KB 14.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 10.6 KB | Display | ![]() |
Images | ![]() | 191.4 KB | ||
Others | ![]() ![]() | 79.2 MB 79.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8fvgMC ![]() 8envC ![]() 8eonC ![]() 8frsC ![]() 8fuvC ![]() 8fvhC C: citing same article ( M: atomic model generated by this map |
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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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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
-Half map: #2
File | emd_29486_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_29486_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Pseudomonas phage vB_PaeM_E217
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Pseudomonas phage vB_PaeM_E217
Supramolecule | Name: Pseudomonas phage vB_PaeM_E217 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 2034346 / Sci species name: Pseudomonas phage vB_PaeM_E217 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: Yes / Virus empty: Yes |
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-Macromolecule #1: Sheath protein gp31
Macromolecule | Name: Sheath protein gp31 / type: protein_or_peptide / ID: 1 / Details: contracted state / Number of copies: 13 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 53.680723 KDa |
Sequence | String: MISQSRYIRI ISGVGAGAPV AGRKLILRVM TTNNVIPPGI VIEFDNANAV LSYFGAQSEE YQRAAAYFKF ISKSVNSPSS ISFARWVNT AIAPMVVGDN LPKTIADFAG FSAGVLTIMV GAAEQNITAI DTSAATSMDN VASIIQTEIR KNADPQLAQA T VTWNQNTN ...String: MISQSRYIRI ISGVGAGAPV AGRKLILRVM TTNNVIPPGI VIEFDNANAV LSYFGAQSEE YQRAAAYFKF ISKSVNSPSS ISFARWVNT AIAPMVVGDN LPKTIADFAG FSAGVLTIMV GAAEQNITAI DTSAATSMDN VASIIQTEIR KNADPQLAQA T VTWNQNTN QFTLVGATIG TGVLAVAKSA DPQDMSTALG WSTSNVVNVA GQSADLPDAA VAKSTNVSNN FGSFLFAGAP LD NDQIKAV SAWNAAQNNQ FIYTVATSLA NLGTLFTLVN GNAGTALNVL SATAANDFVE QCPSEILAAT NYDEPGASQN YMY YQFPGR NITVSDDTVA NTVDKSRGNY IGVTQANGQQ LAFYQRGILC GGPTDAVDMN VYANEIWLKS AIAQALLDLF LNVN AVPAS STGEAMTLAV LQPVLDKATA NGTFTYGKEI SAVQQQYITQ VTGDRRAWRQ VQTLGYWINI TFSSYTNSNT GLTEW KANY TLIYSKGDAI RFVEGSDVMI UniProtKB: Tail sheath protein |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: OTHER / Imaging mode: OTHER / Cs: 2.7 mm / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 81000 |
Sample stage | Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |