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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Helical reconstruction of CHIKV nsP3 helical scaffolds | |||||||||
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![]() | Helical scaffold / Replication complex / Alpha granules / Viral factories / VIRAL PROTEIN | |||||||||
Function / homology | ![]() host cell filopodium / ADP-ribose 1''-phosphate phosphatase / mRNA methyltransferase activity / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide 5'-phosphatase activity / poly(A) RNA polymerase activity / polynucleotide adenylyltransferase / 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 / poly(A) RNA polymerase activity / polynucleotide adenylyltransferase / 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 / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / RNA helicase / 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 | ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 2.35 Å | |||||||||
![]() | Reguera J / Hons M / Zimberger C / Ptchelkine D / Jones R / Desfosses A | |||||||||
Funding support | ![]()
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![]() | ![]() 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 | ![]() | 244.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.7 KB 20.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.4 KB | Display | ![]() |
Images | ![]() | 97.8 KB | ||
Filedesc metadata | ![]() | 6 KB | ||
Others | ![]() ![]() ![]() ![]() ![]() | 201.2 MB 128.3 MB 5.7 MB 239.8 MB 239.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8phzMC ![]() 17729 ![]() 8pk7C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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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
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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: ![]() |
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: 5 / Enantiomer: LEVO / EC number: ADP-ribose 1''-phosphate phosphatase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 57.418207 KDa |
Recombinant expression | Organism: ![]() |
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: 5 / Formula: ZN |
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Molecular weight | Theoretical: 65.409 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | helical array |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE-PROPANE |
Details | his sample was heterogeneous in lenght |
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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: ![]() |
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 |