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Yorodumi- EMDB-37958: Cryo-EM map for Mumps Virus L Protein Bound by Phosphoprotein Tet... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-37958 | |||||||||
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Title | Cryo-EM map for Mumps Virus L Protein Bound by Phosphoprotein Tetramer (Focused map for CD-MTase-CTD) | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Mumps virus polymerase complex / RNA-dependent RNA synthesis / Large protein / phosphoprotein. / VIRAL PROTEIN | |||||||||
Function / homology | Function and homology information GDP polyribonucleotidyltransferase / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / Transferases; Transferring one-carbon groups; Methyltransferases / virion component / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / host cell cytoplasm / hydrolase activity / RNA-directed RNA polymerase / RNA-dependent RNA polymerase activity / ATP binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Mumps orthorubulavirus | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.13 Å | |||||||||
Authors | Li TH / Shen QT | |||||||||
Funding support | China, 1 items
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Citation | Journal: Nat Commun / Year: 2024 Title: Structures of the mumps virus polymerase complex via cryo-electron microscopy. Authors: Tianhao Li / Mingdong Liu / Zhanxi Gu / Xin Su / Yunhui Liu / Jinzhong Lin / Yu Zhang / Qing-Tao Shen / Abstract: The viral polymerase complex, comprising the large protein (L) and phosphoprotein (P), is crucial for both genome replication and transcription in non-segmented negative-strand RNA viruses (nsNSVs), ...The viral polymerase complex, comprising the large protein (L) and phosphoprotein (P), is crucial for both genome replication and transcription in non-segmented negative-strand RNA viruses (nsNSVs), while structures corresponding to these activities remain obscure. Here, we resolved two L-P complex conformations from the mumps virus (MuV), a typical member of nsNSVs, via cryogenic-electron microscopy. One conformation presents all five domains of L forming a continuous RNA tunnel to the methyltransferase domain (MTase), preferably as a transcription state. The other conformation has the appendage averaged out, which is inaccessible to MTase. In both conformations, parallel P tetramers are revealed around MuV L, which, together with structures of other nsNSVs, demonstrates the diverse origins of the L-binding X domain of P. Our study links varying structures of nsNSV polymerase complexes with genome replication and transcription and points to a sliding model for polymerase complexes to advance along the RNA templates. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_37958.map.gz | 305.8 MB | EMDB map data format | |
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Header (meta data) | emd-37958-v30.xml emd-37958.xml | 16 KB 16 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_37958_fsc.xml | 14.6 KB | Display | FSC data file |
Images | emd_37958.png | 45.5 KB | ||
Filedesc metadata | emd-37958.cif.gz | 4.3 KB | ||
Others | emd_37958_additional_1.map.gz emd_37958_half_map_1.map.gz emd_37958_half_map_2.map.gz | 287.7 MB 301.6 MB 301.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-37958 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-37958 | HTTPS FTP |
-Validation report
Summary document | emd_37958_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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Full document | emd_37958_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | emd_37958_validation.xml.gz | 23.3 KB | Display | |
Data in CIF | emd_37958_validation.cif.gz | 30 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-37958 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-37958 | HTTPS FTP |
-Related structure data
Related structure data | 8yxlMC 8izlC 8x01C 8yxmC 8yxoC 8yxpC 8yxrC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_37958.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.53 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Post-processing in deepEMhancer
File | emd_37958_additional_1.map | ||||||||||||
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Annotation | Post-processing in deepEMhancer | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_37958_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_37958_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : The MuV polymerase complex of RNA-directed RNA polymerase L with ...
Entire | Name: The MuV polymerase complex of RNA-directed RNA polymerase L with tetrameric phosphoproteins |
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Components |
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-Supramolecule #1: The MuV polymerase complex of RNA-directed RNA polymerase L with ...
Supramolecule | Name: The MuV polymerase complex of RNA-directed RNA polymerase L with tetrameric phosphoproteins type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 Details: The MuV polymerase complex expressed in Sf9 cells and purified by affinity chromatography and size-exlusive chromatography sequentially. |
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Source (natural) | Organism: Mumps orthorubulavirus / Strain: Jeryl-Lynn |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 1.0 mg/mL | |||||||||||||||
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Buffer | pH: 8 Component:
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average exposure time: 2.75 sec. / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm |
Sample stage | Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |