+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-17729 | |||||||||
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Title | Helical reconstruction of CHIKV nsP3 helical scaffolds | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Helical 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 / mRNA modification / regulation of cytoskeleton organization ...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 / mRNA modification / regulation of cytoskeleton organization / symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity / 7-methylguanosine mRNA capping / cysteine-type peptidase activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 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 innate immune response / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / RNA-directed RNA polymerase / viral RNA genome replication / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / DNA-templated transcription / host cell nucleus / GTP binding / host cell plasma membrane / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding Similarity search - Function | |||||||||
Biological species | Chikungunya virus strain S27-African prototype | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 2.52 Å | |||||||||
Authors | Reguera J / Hons M / Zimberger C / Ptchelkine D / Jones R / Desfosses A | |||||||||
Funding support | France, 2 items
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Citation | Journal: 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 |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_17729.map.gz | 128.3 MB | EMDB map data format | |
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Header (meta data) | emd-17729-v30.xml emd-17729.xml | 15.6 KB 15.6 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_17729_fsc.xml | 13.4 KB | Display | FSC data file |
Images | emd_17729.png | 145.2 KB | ||
Filedesc metadata | emd-17729.cif.gz | 6 KB | ||
Others | emd_17729_half_map_1.map.gz emd_17729_half_map_2.map.gz | 240 MB 240 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17729 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17729 | HTTPS FTP |
-Validation report
Summary document | emd_17729_validation.pdf.gz | 854.1 KB | Display | EMDB validaton report |
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Full document | emd_17729_full_validation.pdf.gz | 853.7 KB | Display | |
Data in XML | emd_17729_validation.xml.gz | 22.4 KB | Display | |
Data in CIF | emd_17729_validation.cif.gz | 29.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17729 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17729 | HTTPS FTP |
-Related structure data
Related structure data | 8pk7MC 8phzC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_17729.map.gz / Format: CCP4 / Size: 259.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_17729_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_17729_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Helical scaffold assembly of CHIKV nsP3 mediated by its Unique al...
Entire | Name: Helical scaffold assembly of CHIKV nsP3 mediated by its Unique alphavirus domain. |
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Components |
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-Supramolecule #1: Helical scaffold assembly of CHIKV nsP3 mediated by its Unique al...
Supramolecule | Name: Helical scaffold assembly of CHIKV nsP3 mediated by its Unique alphavirus domain. type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Chikungunya virus strain S27-African prototype |
Molecular weight | Theoretical: 220.25 kDa/nm |
-Macromolecule #1: Non-structural protein 3
Macromolecule | Name: Non-structural protein 3 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: ADP-ribose 1''-phosphate phosphatase |
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Source (natural) | Organism: Chikungunya virus strain S27-African prototype |
Molecular weight | Theoretical: 57.418207 KDa |
Recombinant expression | Organism: Trichoplusia ni (cabbage looper) |
Sequence | String: 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 |
-Macromolecule #2: ZINC ION
Macromolecule | Name: ZINC ION / type: ligand / ID: 2 / Number of copies: 1 / Formula: ZN |
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Molecular weight | Theoretical: 65.409 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | helical reconstruction |
Aggregation state | helical array |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE-PROPANE |
Details | his sample was heterogeneous in lenght |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 18.1 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination 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 |