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- EMDB-46622: Shigella flexneri bacteriophage Moo19 Icosahedral Reconstruction -
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Open data
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Basic information
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Title | Shigella flexneri bacteriophage Moo19 Icosahedral Reconstruction | |||||||||||||||
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![]() | Moo19 / VIRUS | |||||||||||||||
Function / homology | Phage capsid protein / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Ig-like domain-containing protein / Major capsid protein![]() | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||||||||
![]() | Subramanian S / Bergland Drarvik SM / Parent KN | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Moo19 and B2: Structures of podophages with = 9 geometry and tailspikes with esterase activity. Authors: Sundharraman Subramanian / Silje M Bergland Drarvik / Kendal R Tinney / Sarah M Doore / Kristin N Parent / ![]() Abstract: Podophages are, by far, the least well studied of all the bacteriophages. Despite being classified together due to their short, noncontractile tails, there is a huge amount of diversity among members ...Podophages are, by far, the least well studied of all the bacteriophages. Despite being classified together due to their short, noncontractile tails, there is a huge amount of diversity among members of this group. Of the podophages, the N4-like family is the least well studied structurally and is quite divergent from well-characterized podophages such as T7 and P22. In this work, we isolate and fully characterize two members of the family by cryo-electron microscopy, genetics, and biochemistry. We describe the capsid features of Moo19 and B2, including a decoration protein. In addition, we have fully modeled the tail machinery for both phages and identify proteins with esterase activity. Genetic knockouts of the host reveal factors specific for host attachment including key modifications to the O-antigen on the lipopolysaccharide. Moo19 and B2 are both members, yet some distinct differences in the genome and structure place them into distinct clades. | |||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 265.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.4 KB 17.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 28 KB | Display | ![]() |
Images | ![]() | 304.1 KB | ||
Masks | ![]() | 1.9 GB | ![]() | |
Filedesc metadata | ![]() | 5.8 KB | ||
Others | ![]() ![]() | 1.5 GB 1.5 GB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 765.6 KB | Display | ![]() |
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Full document | ![]() | 765.2 KB | Display | |
Data in XML | ![]() | 35.2 KB | Display | |
Data in CIF | ![]() | 47.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9d7zMC ![]() 9d80C ![]() 9d81C ![]() 9d82C ![]() 9d83C ![]() 9d84C 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: 1.632 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_46622_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_46622_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Shigella virus Moo19
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Shigella virus Moo19
Supramolecule | Name: Shigella virus Moo19 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 2886042 / Sci species name: Shigella virus Moo19 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() |
-Macromolecule #1: Major capsid protein
Macromolecule | Name: Major capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 9 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 43.971672 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MLNYNAPIDG QKSSIDGAGS DQMNTFYWLK KAIIQARKDQ YFMPLASVTN MPKNMGKTIK VYEYVPLLDD RNINDQGIDA NGAHIVNGN LYGSSKDIGT ITSKLPLLTE NGGRVNRVGF TRLSREGSIH KFGFFYEFTQ ESLDFDSDDQ LKEHLSRELM N GAVQITEA ...String: MLNYNAPIDG QKSSIDGAGS DQMNTFYWLK KAIIQARKDQ YFMPLASVTN MPKNMGKTIK VYEYVPLLDD RNINDQGIDA NGAHIVNGN LYGSSKDIGT ITSKLPLLTE NGGRVNRVGF TRLSREGSIH KFGFFYEFTQ ESLDFDSDDQ LKEHLSRELM N GAVQITEA VLQKDLLAAA GTVLYAGAAT SDATITGEGS TPSVITYKNL MRLDAILTDN RTPTQTTIIT GSRLVDTKVI GG TRVMYVG SELVPDLKAM KDLFGNKAFI EIQHYGDAGT LMNGEIGTID KFRIIQVPEM LHWAGAGAAA TDANPGYRTS TVN GTEHYD VYPVLVVGDD SFTTIGFQTD GKSVKFNVMT KMPGKETADR NDPYGETGFS SIKWYYGILV KRPERIAVMK AVAP L UniProtKB: Major capsid protein |
-Macromolecule #2: Ig-like domain-containing protein
Macromolecule | Name: Ig-like domain-containing protein / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 28.133709 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MPELKVAFNK DTYVATVLDA SGSVPSGSVN VGTFFHPDET YPDSYVIYHG VRELLYKRSE VDPAQPGFWP ENITNMQAVT IDNKATARL VLNTSLPRVV STIEGGKVTL SVVALGGKAP LKYKWEFRAP NASTWTAVSG QTTANLVLDN IDADKAGEYK V TVTDAAGT ...String: MPELKVAFNK DTYVATVLDA SGSVPSGSVN VGTFFHPDET YPDSYVIYHG VRELLYKRSE VDPAQPGFWP ENITNMQAVT IDNKATARL VLNTSLPRVV STIEGGKVTL SVVALGGKAP LKYKWEFRAP NASTWTAVSG QTTANLVLDN IDADKAGEYK V TVTDAAGT SVDSTALVAV GAYPPPALTG IKATPTSLSL SVATDAAGKT VALSAIPTDA ELGTLSIKTA PDSARATATI SG STLTVKP VAAGAATSVV VTNGKVDVTI TINVAA UniProtKB: Ig-like 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 Component:
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 33.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |