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- EMDB-30537: Cryo-EM map of Omono River virus (Strain: LZ) full capsid with it... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-30537 | |||||||||
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Title | Cryo-EM map of Omono River virus (Strain: LZ) full capsid with its fiber-like protrusion anchored at the five-fold vertex. | |||||||||
![]() | To show each element of the virus, maps are shown at different counter levels. The major capsid shell: 4%u03C3; Subvolume of the protrusion: 0.65%u03C3. | |||||||||
![]() | Major capsid dimer of OmRV-LZ (with protrusion) != Omono River virus Major capsid dimer of OmRV-LZ (with protrusion)
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Function / homology | Double-stranded RNA binding motif / Double-stranded RNA binding motif / Double stranded RNA-binding domain (dsRBD) profile. / Double-stranded RNA-binding domain / ![]() ![]() | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Shao Q / Jia X | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM reveals a previously unrecognized structural protein of a dsRNA virus implicated in its extracellular transmission. Authors: Qianqian Shao / Xudong Jia / Yuanzhu Gao / Zhe Liu / Huan Zhang / Qiqi Tan / Xin Zhang / Huiqiong Zhou / Yinyin Li / De Wu / Qinfen Zhang / ![]() Abstract: Mosquito viruses cause unpredictable outbreaks of disease. Recently, several unassigned viruses isolated from mosquitoes, including the Omono River virus (OmRV), were identified as totivirus-like ...Mosquito viruses cause unpredictable outbreaks of disease. Recently, several unassigned viruses isolated from mosquitoes, including the Omono River virus (OmRV), were identified as totivirus-like viruses, with features similar to those of the Totiviridae family. Most reported members of this family infect fungi or protozoans and lack an extracellular life cycle stage. Here, we identified a new strain of OmRV and determined high-resolution structures for this virus using single-particle cryo-electron microscopy. The structures feature an unexpected protrusion at the five-fold vertex of the capsid. Disassociation of the protrusion could result in several conformational changes in the major capsid. All these structures, together with some biological results, suggest the protrusions' associations with the extracellular transmission of OmRV. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 771.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.8 KB 13.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 21.1 KB | Display | ![]() |
Images | ![]() | 239.4 KB | ||
Filedesc metadata | ![]() | 6.1 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7d0kMC ![]() 7cz6C ![]() 7d0lC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | To show each element of the virus, maps are shown at different counter levels. The major capsid shell: 4%u03C3; Subvolume of the protrusion: 0.65%u03C3. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.09 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Major capsid dimer of OmRV-LZ (with protrusion)
Entire | Name: Major capsid dimer of OmRV-LZ (with protrusion) |
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Components |
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-Supramolecule #1: Omono River virus
Supramolecule | Name: Omono River virus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 753758 / Sci species name: Omono River virus / Sci species strain: LZ / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() ![]() |
Virus shell | Shell ID: 1 / Name: Major capsid / Diameter: 450.0 Å / T number (triangulation number): 1 |
-Macromolecule #1: Capsid protein
Macromolecule | Name: Capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 96.860992 KDa |
Sequence | String: PISADFSEVE NAPSFLSLAE NTDEVLKPYT GLEIQTIITN IVGDANPNQS RIFDQDRLRG NQYSAGGLVT QNAVSAIPFT NLIPRTIRV GNILVNSANR LQITETNVSE YYSNPIIATK LSEMISDQVK NNQFSTWRRD NTSLQGFNAF DIATINTAIL P NGLSLESM ...String: PISADFSEVE NAPSFLSLAE NTDEVLKPYT GLEIQTIITN IVGDANPNQS RIFDQDRLRG NQYSAGGLVT QNAVSAIPFT NLIPRTIRV GNILVNSANR LQITETNVSE YYSNPIIATK LSEMISDQVK NNQFSTWRRD NTSLQGFNAF DIATINTAIL P NGLSLESM LLKLSLLHSI KAMNVDAASI NRSQYQVIDH NTVPTIGAPA VVGVNNSPVF GEDCGGNNPV YPFGGGTGAI AF HVTLQTV PDERKSYAIF VPPAILQATS DANEALALFA LSMSEWPHAL YTVTKQTTDL AGANAGQQVF IPTQSTIHIG GRR VLDLII PRREIAPNPT TLVAANAMCM VRPQAGPDAT AGAIPLAAGQ LFNMNFIGAP AFEEWPMTSY LYSWAGRFDI TTIR QYMGR LATMVGVKDA YWAAHELNVA LSQVAPKMTT AAGGWAAQAA NSAQQSDVCY SSLLTVTRSA ANFPLANQPA ADMRV YDTD PATWNKVALG LATAANLVPE QSMDVPFVVG DARASFWERL QAIPMCIAWT MYYHSRGITT LAWDNAYTDN TNKWLQ KMV RNTFSTTQSV GTIIPARYGK IVCNLYKNMF HRAPAYVATS VGGKELHITH FERWLPGGTY ANVYSGAGAV VNCFSPV LI PDIWCQYFTA KLPLFAGAFP PAQGQNSTKG FNSKQGLMIH RNQNNNLVAP YLEKFADNSS YFPVGQGPEI NDMATWNG R LWMTTGNVQY LDYSGAAIVE AVPPAGELPV GKQIPLLAGE NAPIELTNAA TTCVPRYSND GRRIFTYLTT AQSVIPVQA CNRAANLARS CWLLSNVYAE PALQALGDEV EDAFDTLTNS SFLDVAKSVA ESAGEVPATK ALTDLQAVDV SSLPSTSDPS NVLSQPAPL MSPPTSSS |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 Component:
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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY | |||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Sample stage | Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average electron dose: 39.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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Output model | ![]() PDB-7d0k: |