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- EMDB-37528: MPOX E5 hexamer ssDNA bound apo conformation -

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Basic information

Entry
Database: EMDB / ID: EMD-37528
TitleMPOX E5 hexamer ssDNA bound apo conformation
Map datamainmap
Sample
  • Complex: MPOX helicase
    • Protein or peptide: Uncoating factor OPG117
    • DNA: DNA (5'-D(P*CP*CP*CP*C)-3')
KeywordsMonkey pox / helicase / DNA replication / Complex / VIRAL PROTEIN / DNA BINDING PROTEIN-DNA complex
Function / homologyDNA 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. / hydrolase activity / P-loop containing nucleoside triphosphate hydrolase / Uncoating factor OPG117
Function and homology information
Biological speciesMonkeypox virus / Spodoptera frugiperda (fall armyworm)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.03 Å
AuthorsZhang Z / Dong C
Funding support China, 1 items
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, 2023-
Header (metadata) releaseSep 25, 2024-
Map releaseSep 25, 2024-
UpdateSep 25, 2024-
Current statusSep 25, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_37528.png

Downloads & links

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Map

FileDownload / File: emd_37528.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationmainmap
Projections & slices

Image control

Size
Brightness
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AxesZ (Sec.)Y (Row.)X (Col.)
0.84 Å/pix.
x 320 pix.
= 268.8 Å		0.84 Å/pix.
x 320 pix.
= 268.8 Å		0.84 Å/pix.
x 320 pix.
= 268.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.84 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.06
Minimum - Maximum-0.8651974 - 1.4062517
Average (Standard dev.)0.00087282545 (±0.026911559)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 268.8 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_37528_msk_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: halfmapA

Fileemd_37528_half_map_1.map
AnnotationhalfmapA
Projections & Slices
AxesZYX

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Density Histograms

Histogram

Histogram (log scale)

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Half map: halfmapB

Fileemd_37528_half_map_2.map
AnnotationhalfmapB
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Sample components

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Entire : MPOX helicase

EntireName: MPOX helicase
Components
  • Complex: MPOX helicase
    • Protein or peptide: Uncoating factor OPG117
    • DNA: DNA (5'-D(P*CP*CP*CP*C)-3')

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Supramolecule #1: MPOX helicase

SupramoleculeName: MPOX helicase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: MPOX helicase apo form
Source (natural)Organism: Monkeypox virus

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Macromolecule #1: Uncoating factor OPG117

MacromoleculeName: Uncoating factor OPG117 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Monkeypox virus
Molecular weightTheoretical: 90.476344 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MDAAIRGNDV IFVLKTIGVP SACRQNEDPR FVEAFKCDEL ERYIDNNPEC TLFESLRDEE AYSIVRIFMD VDLDACLDEI DYLTAIQDF IIEVSNCVAR FAFTECGAIH ENVIKSMRSN FSLTKSTNRD KTSFHIIFLD TYTTMDTLIA MKRTLLELSR S SENPLTRS ...String:
MDAAIRGNDV IFVLKTIGVP SACRQNEDPR FVEAFKCDEL ERYIDNNPEC TLFESLRDEE AYSIVRIFMD VDLDACLDEI DYLTAIQDF IIEVSNCVAR FAFTECGAIH ENVIKSMRSN FSLTKSTNRD KTSFHIIFLD TYTTMDTLIA MKRTLLELSR S SENPLTRS IDTAVYRRKT TLRVVGTRKN PNCDTIHVMQ PPHDNIEDYL FTYVDMNNNS YYFSLQRRLE DLVPDKLWEP GF ISFEDAI KRVSKIFINS IINFNDLDEN NFTTVPLVID YVTPCALCKK RSHKHPHQLS LENGAIRIYK TGNPHSCKVK IVP LDGNKL FNIAQRILDT NSVLLTERGD HIVWINNSWK FNSEEPLITK LILSIRHQLP KEYSSELLCP RKRKTVEANI RDML VDSVE TDTYPDKLPF KNGVLDLVDG MFYSGDDAKK YTCTVSTGFK FDDTKFVEDS PEMEELMNII NDIQPLTDEN KKNRE LYEK TLSSCLCGAT KGCLTFFFGE TATGKSTTKR LLKSAIGDLF VETGQTILTD VLDKGPNPFI ANMHLKRSVF CSELPD FAC SGSKKIRSDN IKKLTEPCVI GRPCFSNKIN NRNHATIIID TNYKPVFDRI DNALMRRIAV VRFRTHFSQP SGREAAE NN DAYDKVKLLD EGLDGKIQNN RYRFAFLYLL VKWYKKYHIP IMKLYPTPEE IPDFAFYLKI GTLLVSSSVK HIPLMTDL S KKGYILYDNV VTLPLTTFQQ KISKYFNSRL FGHDIESFIN RHKKFANVSD EYLQYIFIED ISSP

UniProtKB: Uncoating factor OPG117

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Macromolecule #2: DNA (5'-D(P*CP*CP*CP*C)-3')

MacromoleculeName: DNA (5'-D(P*CP*CP*CP*C)-3') / type: dna / ID: 2 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Spodoptera frugiperda (fall armyworm)
Molecular weightTheoretical: 1.11177 KDa
SequenceString:
(DC)(DC)(DC)(DC)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration1 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE
Detailsquantifoil 1.2/1.3 Cu

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.03 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 263224
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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