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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | African swine fever virus RNA Polymerase--DNA complex | |||||||||
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![]() | ASFV / RNA polymerase / VIRAL PROTEIN | |||||||||
Function / homology | ![]() viral transcription / transcription elongation by RNA polymerase I / tRNA transcription by RNA polymerase III / DNA-directed RNA polymerase activity / DNA-directed RNA polymerase complex / ribonucleoside binding / virion component / : / : / : ...viral transcription / transcription elongation by RNA polymerase I / tRNA transcription by RNA polymerase III / DNA-directed RNA polymerase activity / DNA-directed RNA polymerase complex / ribonucleoside binding / virion component / : / : / : / : / : / : / DNA-directed RNA polymerase / host cell cytoplasm / protein dimerization activity / DNA-templated transcription / DNA binding / zinc ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.78 Å | |||||||||
![]() | Feng XY | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Transcription regulation of African swine fever virus: dual role of M1249L. Authors: Dongming Zhao / Nan Wang / Xiaoying Feng / Zhenjiang Zhang / Kongen Xu / Tao Zheng / Yunge Yang / Xuemei Li / Xianjin Ou / Rui Zhao / Zihe Rao / Zhigao Bu / Yutao Chen / Xiangxi Wang / ![]() Abstract: African swine fever virus (ASFV), which poses significant risks to the global economy, encodes a unique host-independent transcription system. This system comprises an eight-subunit RNA polymerase ...African swine fever virus (ASFV), which poses significant risks to the global economy, encodes a unique host-independent transcription system. This system comprises an eight-subunit RNA polymerase (vRNAP), temporally expressed transcription factors and transcript associated proteins, facilitating cross-species transmission via intermediate host. The protein composition of the virion and the presence of transcription factors in virus genome suggest existence of distinct transcription systems during viral infection. However, the precise mechanisms of transcription regulation remain elusive. Through analyses of dynamic transcriptome, vRNAP-associated components and cell-based assay, the critical role of M1249L in viral transcription regulation has been highlighted. Atomic-resolution structures of vRNAP-M1249L supercomplex, exhibiting a variety of conformations, have uncovered the dual functions of M1249L. During early transcription, M1249L could serve as multiple temporary transcription factors with C-terminal domain acting as a switcher for activation/inactivation, while during late transcription it aids in the packaging of the transcription machinery. The structural and functional characteristics of M1249L underscore its vital roles in ASFV transcription, packaging, and capsid assembly, presenting novel opportunities for therapeutic intervention. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 116.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 26.9 KB 26.9 KB | Display Display | ![]() |
Images | ![]() | 27.1 KB | ||
Filedesc metadata | ![]() | 8.6 KB | ||
Others | ![]() ![]() | 98.2 MB 98.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8yqzMC ![]() 8yqtC ![]() 8yquC ![]() 8yqvC ![]() 8yqwC ![]() 8yqxC ![]() 8yqyC 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: 0.808 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_39511_half_map_1.map | ||||||||||||
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Density Histograms |
-Half map: #1
File | emd_39511_half_map_2.map | ||||||||||||
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Sample components
+Entire : African swine fever virus RNA polymerase complex
+Supramolecule #1: African swine fever virus RNA polymerase complex
+Macromolecule #1: DNA-directed RNA polymerase subunit
+Macromolecule #2: DNA-directed RNA polymerase subunit beta
+Macromolecule #3: DNA-directed RNA polymerase RPB3-11 homolog
+Macromolecule #4: DNA-directed RNA polymerase RPB5 homolog
+Macromolecule #5: C147L
+Macromolecule #6: D339L
+Macromolecule #7: C122R
+Macromolecule #8: DNA-directed RNA polymerase RPB10 homolog
+Macromolecule #9: DNA (5'-D(P*GP*CP*CP*GP*AP*GP*CP*A)-3')
+Macromolecule #10: DNA (5'-D(P*TP*CP*GP*GP*CP*TP*C)-3')
+Macromolecule #11: MAGNESIUM ION
+Macromolecule #12: ZINC ION
-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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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 1.25 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |