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- PDB-8wh4: MPOX E5 hexamer ssDNA bound apo conformation -

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Basic information

Entry
Database: PDB / ID: 8wh4
TitleMPOX E5 hexamer ssDNA bound apo conformation
Components
  • DNA (5'-D(P*CP*CP*CP*C)-3')
  • Uncoating factor OPG117
KeywordsDNA BINDING PROTEIN/DNA / Monkey pox / helicase / DNA replication / Complex / VIRAL PROTEIN / DNA BINDING PROTEIN-DNA complex
Function / homology
Function and homology information


helicase activity / hydrolase activity
Similarity search - Function
DNA primase/nucleoside triphosphatase, C-terminal / Poxvirus D5 protein-like / : / Bacteriophage/plasmid primase, P4, C-terminal / D5 N terminal like / Helicase, superfamily 3, DNA virus / Superfamily 3 helicase of DNA viruses domain profile. / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
DNA / Uncoating factor OPG117
Similarity search - Component
Biological speciesMonkeypox virus
Spodoptera frugiperda (fall armyworm)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.03 Å
AuthorsZhang, Z. / Dong, C.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32371303 China
CitationJournal: Sci Adv / Year: 2024
Title: Essential and multifunctional mpox virus E5 helicase-primase in double and single hexamer.
Authors: Yunxia Xu / Yaqi Wu / Yuanyuan Zhang / Kaiting Gao / Xiaoying Wu / Yaxue Yang / Danyang Li / Biao Yang / Zhengyu Zhang / Changjiang Dong /
Abstract: An outbreak of mpox virus in May 2022 has spread over 110 nonpandemic regions in the world, posing a great threat to global health. Mpox virus E5, a helicase-primase, plays an essential role in DNA ...An outbreak of mpox virus in May 2022 has spread over 110 nonpandemic regions in the world, posing a great threat to global health. Mpox virus E5, a helicase-primase, plays an essential role in DNA replication, but the molecular mechanisms are elusive. Here, we report seven structures of mpox virus E5 in a double hexamer (DH) and six in single hexamer in different conformations, indicating a rotation mechanism for helicase and a coupling action for primase. The DH is formed through the interface of zinc-binding domains, and the central channel density indicates potential double-stranded DNA (dsDNA), which helps to identify dsDNA binding residues Arg, Lys, Lys, and Lys. Our work is important not only for understanding poxviral DNA replication but also for the development of novel therapeutics for serious poxviral infections including smallpox virus and mpox virus.
History
DepositionSep 22, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 25, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Uncoating factor OPG117
B: Uncoating factor OPG117
C: Uncoating factor OPG117
D: Uncoating factor OPG117
E: Uncoating factor OPG117
F: Uncoating factor OPG117
T: DNA (5'-D(P*CP*CP*CP*C)-3')


Theoretical massNumber of molelcules
Total (without water)543,9707
Polymers543,9707
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein
Uncoating factor OPG117


Mass: 90476.344 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Monkeypox virus / Gene: E5R / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q5IXS3
#2: DNA chain DNA (5'-D(P*CP*CP*CP*C)-3')


Mass: 1111.770 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Spodoptera frugiperda (fall armyworm)

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: MPOX helicase / Type: COMPLEX / Details: MPOX helicase apo form / Entity ID: all / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Monkeypox virus
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 7.5
SpecimenConc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: quantifoil 1.2/1.3 Cu
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

CTF correctionType: NONE
3D reconstructionResolution: 3.03 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 263224 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00822841
ELECTRON MICROSCOPYf_angle_d0.80930892
ELECTRON MICROSCOPYf_dihedral_angle_d6.6273043
ELECTRON MICROSCOPYf_chiral_restr0.0423472
ELECTRON MICROSCOPYf_plane_restr0.0073940

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