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- PDB-9jkc: Crystal structure of Aspergillus fumigatus polymycovirus 1 ployme... -

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Basic information

Entry
Database: PDB / ID: 9jkc
TitleCrystal structure of Aspergillus fumigatus polymycovirus 1 ploymerase (residues 85-763) in its apo state
ComponentsRNA dependent RNA polymerase
KeywordsVIRAL PROTEIN / RNA virus / RNA-dependent RNA polymerase
Function / homology
Function and homology information


viral RNA genome replication / RNA-directed RNA polymerase activity / DNA-templated transcription / RNA binding
Similarity search - Function
RNA-directed RNA polymerase, C-terminal domain / Viral RNA-dependent RNA polymerase / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / DNA/RNA polymerase superfamily
Similarity search - Domain/homology
RNA dependent RNA polymerase
Similarity search - Component
Biological speciesAspergillus fumigatus tetramycovirus 1
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.4 Å
AuthorsJia, H. / Cao, S. / Gong, P.
Funding support China, 2items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2018YFA0507200 China
National Natural Science Foundation of China (NSFC)32300139 China
CitationJournal: Sci Adv / Year: 2025
Title: An evolutionarily unique viral RdRP suggests a common dual-function feature of the priming element.
Authors: Jia, H. / Liu, S. / Rao, G. / Liu, Q. / Wu, J. / Cao, S. / Gong, P.
History
DepositionSep 15, 2024Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Mar 26, 2025Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2025Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: RNA dependent RNA polymerase
B: RNA dependent RNA polymerase
C: RNA dependent RNA polymerase
D: RNA dependent RNA polymerase
E: RNA dependent RNA polymerase


Theoretical massNumber of molelcules
Total (without water)384,5665
Polymers384,5665
Non-polymers00
Water52229
1
A: RNA dependent RNA polymerase


Theoretical massNumber of molelcules
Total (without water)76,9131
Polymers76,9131
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: RNA dependent RNA polymerase


Theoretical massNumber of molelcules
Total (without water)76,9131
Polymers76,9131
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: RNA dependent RNA polymerase


Theoretical massNumber of molelcules
Total (without water)76,9131
Polymers76,9131
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: RNA dependent RNA polymerase


Theoretical massNumber of molelcules
Total (without water)76,9131
Polymers76,9131
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: RNA dependent RNA polymerase


Theoretical massNumber of molelcules
Total (without water)76,9131
Polymers76,9131
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)257.961, 182.916, 118.681
Angle α, β, γ (deg.)90.000, 103.790, 90.000
Int Tables number5
Space group name H-MC121

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Components

#1: Protein
RNA dependent RNA polymerase


Mass: 76913.234 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aspergillus fumigatus tetramycovirus 1 / Gene: RdRP / Plasmid: pET26b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-CodonPlus(DE3)-RIL / References: UniProt: A0A0H5BRR0
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 29 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.54 Å3/Da / Density % sol: 65.21 %
Crystal growTemperature: 289 K / Method: evaporation / pH: 8.5 / Details: Tris pH 8.5, SOKALAN CP 42

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.97917 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 11, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97917 Å / Relative weight: 1
ReflectionResolution: 3.4→40 Å / Num. obs: 72936 / % possible obs: 99.8 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.141 / Rpim(I) all: 0.09 / Rrim(I) all: 0.168 / Χ2: 0.891 / Net I/σ(I): 8 / Num. measured all: 245809
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
3.4-3.523.20.49272730.750.3240.5920.82699.8
3.52-3.663.40.38572310.8410.2430.4570.8199.7
3.66-3.833.50.27972990.9180.1760.330.808100
3.83-4.033.40.21972960.9450.140.2610.88199.9
4.03-4.283.30.15672620.970.1030.1880.887100
4.28-4.613.50.12672850.9810.0790.1490.94100
4.61-5.083.40.09873270.9870.0620.1160.965100
5.08-5.813.30.10172970.9870.0650.1210.94499.9
5.81-7.313.40.07973330.9910.050.0941.022100
7.31-403.20.03973330.9970.0250.0460.82298.7

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Processing

Software
NameVersionClassification
HKL-2000data scaling
PHENIX1.19refinement
PDB_EXTRACT3.27data extraction
HKL-2000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: Cyro-EM structure of AfuPmV-1 N85

Resolution: 3.4→29.88 Å / SU ML: 0.34 / Cross valid method: THROUGHOUT / σ(F): 1.37 / Phase error: 20.56 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2056 3723 5.11 %
Rwork0.1576 69154 -
obs0.1601 72877 99.38 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 124.86 Å2 / Biso mean: 47.7779 Å2 / Biso min: 18.06 Å2
Refinement stepCycle: final / Resolution: 3.4→29.88 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms25253 0 0 29 25282
Biso mean---31.23 -
Num. residues----3292
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 27

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.4-3.440.30991210.24452300242188
3.44-3.490.27831390.228425272666100
3.49-3.540.29971460.208625252671100
3.54-3.590.29121650.21112585275099
3.59-3.640.24711260.187925362662100
3.64-3.70.22851520.182425792731100
3.7-3.760.23751610.170425202681100
3.76-3.820.21741290.16525842713100
3.82-3.890.23331260.162525762702100
3.89-3.970.20941050.165126172722100
3.97-4.050.21461260.157525712697100
4.05-4.130.21661220.15425622684100
4.13-4.230.1931530.141925692722100
4.23-4.340.17991220.14625522674100
4.34-4.450.17561320.142426062738100
4.45-4.580.21081430.141525642707100
4.58-4.730.19041660.133625472713100
4.73-4.90.18271500.136125532703100
4.9-5.090.17671340.132226062740100
5.09-5.330.18641400.143325442684100
5.33-5.60.22441560.166725892745100
5.6-5.950.22671260.161225792705100
5.95-6.410.21271240.156626032727100
6.41-7.040.19981260.160826012727100
7.05-8.050.16971450.13925912736100
8.05-10.070.1451470.115725862733100
10.07-29.880.16841410.16222582272397

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