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Open data
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Basic information
Entry | ![]() | |||||||||||||||
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Title | Shigella flexneri bacteriophage B2 Gp48 and Gp49 | |||||||||||||||
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![]() | B2 / Gp48 & Gp49 / VIRAL PROTEIN | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.4 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 | ![]() | 346.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.9 KB 16.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 18.4 KB | Display | ![]() |
Images | ![]() | 119.9 KB | ||
Masks | ![]() | 669.9 MB | ![]() | |
Filedesc metadata | ![]() | 6.3 KB | ||
Others | ![]() ![]() | 621.6 MB 621.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9d84MC ![]() 9d7zC ![]() 9d80C ![]() 9d81C ![]() 9d82C ![]() 9d83C M: atomic model generated by this map C: citing same article ( |
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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: 0.886 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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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_46628_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_46628_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Shigella phage B2
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Shigella phage B2
Supramolecule | Name: Shigella phage B2 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 2968270 / Sci species name: Shigella phage B2 / Virus type: VIRION / Virus isolate: OTHER / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() |
-Macromolecule #1: Gp48
Macromolecule | Name: Gp48 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 83.297094 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MNQLFSQGGK GSAGILTNKQ AVARHFGVKQ SEVVYFSVGV DISGYKVIYD KTTQRAYSLP IGIPAGTTAI SLSTAAVLVH SQGSVDLGA VAVLRKEYVT IPGDFTSGAT IQVKNEILTH SNGAQYRWAG AVPKVVPAGS TPASSGGISA SAWIEVTGEE L RDELATTG ...String: MNQLFSQGGK GSAGILTNKQ AVARHFGVKQ SEVVYFSVGV DISGYKVIYD KTTQRAYSLP IGIPAGTTAI SLSTAAVLVH SQGSVDLGA VAVLRKEYVT IPGDFTSGAT IQVKNEILTH SNGAQYRWAG AVPKVVPAGS TPASSGGISA SAWIEVTGEE L RDELATTG GASQIGTSDG KTVQQWIIAN DSANYRARNI QKLAWVDKQV HSRGSIKVLF QGDSMTAGYD TTSTDRVPAN NG DWATHAS MTYPQRFMAY LPEQSGCSVT GVYRAISGHT AIQSYNEPSW QSNPNCDVVI LMLGLNDAGG VAGTTEDIYM EYM EKLIRR FIDWGMGVVV QTCSTGGQGS GGVVANLWAK RMRMMADTYG CAHFNADEVQ YYRHNGAVQS DGGHFNSMGY AIHG QMLAS MFMAGGLLPT YRPLTNEINT WCGRLDDSIG YCDATGNINL GRSDGAYTRT KVVGGMLANV ASIATFSFYL DAEAA HIFV HGSGAGPINV LVDAPSWWNN GAQDYYDFAN NQSINFSNSP QAANNAIVDL STTYSADRKF VGRILGRGWK TLTFFT NLQ GTGGDFYLNS LTVQPVPVGM SVQARNWARF DKGHRAVYSK KIPQAYNQAT LPTATALVNF QVPMPQSMLP TTPSISG DL GTNFYNCGHS VLKISNSSGD YLEVLLIKTT GGGYVFTGKI LKTTYATGNQ PTAITATAAH YSMKDLKVAG ANGPNMPL E TIRDIDMASY VTIGVGAGNG GLVLDINITW PSTPPTSYWN IELEAWDMFG NSEASI |
-Macromolecule #2: Gp49
Macromolecule | Name: Gp49 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 44.471602 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MIRTTNTCCG NQAGMVEKFI GTAYDVVKTV YDNLGEIQFI YNFLNDYGVL ITVDSVTELQ ELPTTAKYTR VYSSTPTGVR IYTDYLYVE GDRTGVLPSD PTATGSWVVV GSSNSGAATG TGAYIPFVFN NGSAAGGETT IVVPDYTIGV PEIYVEGFRQ Q VGRGFTFN ...String: MIRTTNTCCG NQAGMVEKFI GTAYDVVKTV YDNLGEIQFI YNFLNDYGVL ITVDSVTELQ ELPTTAKYTR VYSSTPTGVR IYTDYLYVE GDRTGVLPSD PTATGSWVVV GSSNSGAATG TGAYIPFVFN NGSAAGGETT IVVPDYTIGV PEIYVEGFRQ Q VGRGFTFN SVNLTVTLAQ PLEQGDEVVL MLSGNPAVPD NPNIDSWTVI NWIYNNGAAV GGEQVIVIPY TFQTVPAIFK NG LRYQGGL STQSYTVDQD NKRILLTEPL STNDRLVVQL GGELVTLESP DRSLYEIARA TNMKDSEVIK SDNTVETLNG KRI LYDIVS QVYYWIPSSV PNNVYIQSVV NGQLTYLPGN IVVTLTPIVT LGLSGTTAQR PIGVLTGTQH FDTTLGKPIW FNGT AWVDS TGAVV |
-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 TALOS ARCTICA |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 43.14 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.1 µm / Nominal defocus min: 0.7000000000000001 µm |
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |