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Open data
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Basic information
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Title | Midsection of bacteriophage Mycofy1 mature head (C5 symmetry) | |||||||||
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![]() | Mycobacterium / bacteriophage / prolate head / major capsid protein / VIRUS / VIRAL PROTEIN | |||||||||
Function / homology | : / Phage capsid / Phage capsid family / virion component / Phage capsid-like C-terminal domain-containing protein![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.52 Å | |||||||||
![]() | Li X / Shao Q / Li L / Xie L / Ruan Z / Fang Q | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM Reveals Structural Diversity in Prolate-headed Mycobacteriophage Mycofy1. Authors: Xiangyun Li / Qianqian Shao / Lin Li / Linlin Xie / Zhiyang Ruan / Qianglin Fang / ![]() Abstract: Mycobacteriophages show promise in treating antibiotic-resistant mycobacterial infections. Here, we isolated Mycofy1, a mycobacteriophage, using M. smegmatis as a host. Cryo-EM analysis revealed that ...Mycobacteriophages show promise in treating antibiotic-resistant mycobacterial infections. Here, we isolated Mycofy1, a mycobacteriophage, using M. smegmatis as a host. Cryo-EM analysis revealed that Mycofy1 possesses a prolate head and a long non-contractile tail. We determined structures of its head, head-to-tail interface, terminator, and tail tube to resolutions of ∼3.5 Å. Unexpectedly, we identified two distinct types of prolate head structures, exhibiting a 36° relative rotation in the top cap region. Additionally, the head-to-tail interface demonstrated flexibility. Our structures provide high-resolution cryo-EM data of a mycobacteriophage with a prolate head, as well as detailed structural information of the head-to-tail interface and head-proximal tail region in this phage group. These findings advance our understanding of assembly mechanisms in tailed bacteriophages. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 440.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17 KB 17 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 17.5 KB | Display | ![]() |
Images | ![]() | 204.9 KB | ||
Masks | ![]() | 476.8 MB | ![]() | |
Filedesc metadata | ![]() | 6 KB | ||
Others | ![]() ![]() | 381.4 MB 381.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9lw7MC ![]() 9lw6C ![]() 9lw8C ![]() 9lw9C ![]() 9lwaC 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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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.6464 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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-Half map: #2
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-Half map: #1
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Sample components
-Entire : Mycolicibacterium phage Mycofy1
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Mycolicibacterium phage Mycofy1
Supramolecule | Name: Mycolicibacterium phage Mycofy1 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 3349809 / Sci species name: Mycolicibacterium phage Mycofy1 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() |
-Macromolecule #1: Phage capsid-like C-terminal domain-containing protein
Macromolecule | Name: Phage capsid-like C-terminal domain-containing protein type: protein_or_peptide / ID: 1 Details: Sequence reference for Mycolicibacterium phage Mycofy1 is not available at the time of biocuration. Current sequence reference is from UniProt id Q854Z2. Number of copies: 12 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 59.777262 KDa |
Sequence | String: MNTLDTLPVH PRTGLRAIGM GKRGPIWPVM GASDDHKDDA PTLTYSQARN RADEVHARME QIAELDKPTD EENEEFRALG AEFDSLVNH MSRLERAAEL ARVRSTHEQI GKPQSGGQRR MRVEAGSSQG GRGDYDRDAI LEPDSIEDCR FRDPWNLSEM R TFGRDAEE ...String: MNTLDTLPVH PRTGLRAIGM GKRGPIWPVM GASDDHKDDA PTLTYSQARN RADEVHARME QIAELDKPTD EENEEFRALG AEFDSLVNH MSRLERAAEL ARVRSTHEQI GKPQSGGQRR MRVEAGSSQG GRGDYDRDAI LEPDSIEDCR FRDPWNLSEM R TFGRDAEE VKGELRARAL SAIEKMQGAS DNVRAAATHI IERFDDEDST LARQCLATSS PAYLRAWSKM ARNPHAAILT EE EKRAINE VRAMGLTKAD GGYLVPFQLD PTVIITSNGS LNDIRRFARQ VVATGDVWHG VSSAAVQWSW DAEFEEVSDD SPE FGQPEI PVKKAQGFVP ISIEALQDEA NVTETVALLF AEGKDELEAV TLTTGTGQGN QPTGIVTALA GTAAEIAPVT AETF ALADV YAVYEQLAAR HRRQGAWLAN NLIYNKIRQF DTQGGAGLWT TIGNGEPSQL LGRPVGEAEA MDANWNTSAS ADNFV LLYG NFQNYVIADR IGMTVEFIPH LFGTNRRPNG SRGWFAYYRM GADVVNPNAF RLLNVETAS UniProtKB: Phage capsid-like C-terminal 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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Grid | Model: Quantifoil R2/1 / Material: COPPER / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS KRIOS |
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Software | Name: EPU |
Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average exposure time: 5.09 sec. / Average electron dose: 25.7 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 / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 59000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |