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- EMDB-17729: Helical reconstruction of CHIKV nsP3 helical scaffolds -

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Basic information

Entry
Database: EMDB / ID: EMD-17729
TitleHelical reconstruction of CHIKV nsP3 helical scaffolds
Map data
Sample
  • Complex: Helical scaffold assembly of CHIKV nsP3 mediated by its Unique alphavirus domain.
    • Protein or peptide: Non-structural protein 3
  • Ligand: ZINC ION
KeywordsHelical scaffold / Replication complex / Alpha granules / Viral factories / VIRAL PROTEIN
Function / homology
Function and homology information


host cell filopodium / ADP-ribose 1''-phosphate phosphatase / mRNA methyltransferase activity / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide 5'-phosphatase activity / polynucleotide adenylyltransferase / poly(A) RNA polymerase activity / regulation of cytoskeleton organization / symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity ...host cell filopodium / ADP-ribose 1''-phosphate phosphatase / mRNA methyltransferase activity / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide 5'-phosphatase activity / polynucleotide adenylyltransferase / poly(A) RNA polymerase activity / regulation of cytoskeleton organization / symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity / 7-methylguanosine mRNA capping / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / cysteine-type peptidase activity / Transferases; Transferring one-carbon groups; Methyltransferases / host cell cytoplasmic vesicle membrane / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / nucleoside-triphosphate phosphatase / methylation / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / RNA helicase / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont-mediated suppression of host innate immune response / RNA-directed RNA polymerase / viral RNA genome replication / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / DNA-templated transcription / GTP binding / host cell nucleus / host cell plasma membrane / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding
Similarity search - Function
: / : / : / Non-structural protein 3, zinc-binding domain / Tomato mosaic virus helicase, N-terminal domain / Alphavirus nsp2 protease (nsp2pro) domain / Alphavirus nsP2 protease domain superfamily / Peptidase family C9 / Alphavirus nsp2 protease (nsp2pro) domain profile. / Viral methyltransferase ...: / : / : / Non-structural protein 3, zinc-binding domain / Tomato mosaic virus helicase, N-terminal domain / Alphavirus nsp2 protease (nsp2pro) domain / Alphavirus nsP2 protease domain superfamily / Peptidase family C9 / Alphavirus nsp2 protease (nsp2pro) domain profile. / Viral methyltransferase / Alphavirus-like methyltransferase (MT) domain / Alphavirus-like methyltransferase (MT) domain profile. / Tymovirus, RNA-dependent RNA polymerase / RNA dependent RNA polymerase / Viral (Superfamily 1) RNA helicase / (+) RNA virus helicase core domain / (+)RNA virus helicase core domain profile. / Non-structural protein 3, X-domain-like / Macro domain / Appr-1"-p processing enzyme / Macro domain / Macro domain profile. / Macro domain-like / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / S-adenosyl-L-methionine-dependent methyltransferase superfamily / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Biological speciesChikungunya virus strain S27-African prototype
Methodhelical reconstruction / cryo EM / Resolution: 2.52 Å
AuthorsReguera J / Hons M / Zimberger C / Ptchelkine D / Jones R / Desfosses A
Funding support France, 2 items
OrganizationGrant numberCountry
Agence Nationale de la Recherche (ANR)ANR-22-CE11-0023-01 France
ATIP-Avenir2015 France
CitationJournal: To Be Published
Title: The alphavirus nsP3 protein forms helical tubular scaffolds important for viral replication and particle assembly
Authors: Reguera J / Hons M / Zimberger C / Ptchelkine D / Jones R / Desfosses A
History
DepositionJun 25, 2023-
Header (metadata) releaseAug 14, 2024-
Map releaseAug 14, 2024-
UpdateAug 14, 2024-
Current statusAug 14, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_17729.png

Downloads & links

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Map

FileDownload / File: emd_17729.map.gz / Format: CCP4 / Size: 259.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 408 pix.
= 432.48 Å		1.06 Å/pix.
x 408 pix.
= 432.48 Å		1.06 Å/pix.
x 408 pix.
= 432.48 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.331
Minimum - Maximum-0.21537532 - 0.9733369
Average (Standard dev.)0.003688323 (±0.048842713)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions408408408
Spacing408408408
CellA=B=C: 432.47998 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_17729_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_17729_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Helical scaffold assembly of CHIKV nsP3 mediated by its Unique al...

EntireName: Helical scaffold assembly of CHIKV nsP3 mediated by its Unique alphavirus domain.
Components
  • Complex: Helical scaffold assembly of CHIKV nsP3 mediated by its Unique alphavirus domain.
    • Protein or peptide: Non-structural protein 3
  • Ligand: ZINC ION

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Supramolecule #1: Helical scaffold assembly of CHIKV nsP3 mediated by its Unique al...

SupramoleculeName: Helical scaffold assembly of CHIKV nsP3 mediated by its Unique alphavirus domain.
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Chikungunya virus strain S27-African prototype
Molecular weightTheoretical: 220.25 kDa/nm

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Macromolecule #1: Non-structural protein 3

MacromoleculeName: Non-structural protein 3 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: ADP-ribose 1''-phosphate phosphatase
Source (natural)Organism: Chikungunya virus strain S27-African prototype
Molecular weightTheoretical: 57.418207 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: APSYRVKRMD IAKNDEECVV NAANPRGLPG DGVCKAVYKK WPESFKNSAT PVGTAKTVMC GTYPVIHAVG PNFSNYSESE GDRELAAAY REVAKEVTRL GVNSVAIPLL STGVYSGGKD RLTQSLNHLF TAMDSTDADV VIYCRDKEWE KKISEAIQMR T QVELLDEH ...String:
APSYRVKRMD IAKNDEECVV NAANPRGLPG DGVCKAVYKK WPESFKNSAT PVGTAKTVMC GTYPVIHAVG PNFSNYSESE GDRELAAAY REVAKEVTRL GVNSVAIPLL STGVYSGGKD RLTQSLNHLF TAMDSTDADV VIYCRDKEWE KKISEAIQMR T QVELLDEH ISIDCDVVRV HPDSSLAGRK GYSTTEGALY SYLEGTRFHQ TAVDMAEIYT MWPKQTEANE QVCLYALGES IE SIRQKCP VDDADASSPP KTVPCLCRYA MTPERVTRLR MNHVTSIIVC SSFPLPKYKI EGVQKVKCSK VMLFDHNVPS RVS PREYRP SQESVQEAST TTSLTHSQFD LSVDGKILPV PSDLDADAPA LEPALDDGAI HTLPSATGNL AAVSDWVMST VPVA PPRRR RGRNLTVTCD EREGNITPMA SVRFFRAELC PVVQETAETR DTAMSLQAPP STATELSHPP ISFGAPSETF PITFG DFNE GEIESLSSEL LTFGDFLPGE VDDLTDSDWS TCSDTDDEL

UniProtKB: Polyprotein P1234

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Macromolecule #2: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 2 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statehelical array

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE-PROPANE
Detailshis sample was heterogeneous in lenght

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 18.1 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: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 2.782 Å
Applied symmetry - Helical parameters - Δ&Phi: -164.175 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 2.52 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC
Details: The assembly was calculated from the helical reconstruction of nsP3 from PDB 8PHZ subunit A. This was refined on a local refinement map at 2.35 A resolution
Number images used: 807973
Startup modelType of model: INSILICO MODEL
In silico model: Alphafold2 (Colabfold) was used to have a model of the CHIKV AUD domain
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

8phz


Chain - Chain ID: A / Chain - Residue range: 174-600 / Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementProtocol: AB INITIO MODEL
Output model

PDB-8pk7:
Helical reconstruction of CHIKV nsP3 helical scaffolds

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