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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-30279 | |||||||||
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| Title | Helical reconstruction of Zika virus complexed with Fab C10 | |||||||||
Map data | helical reconstruction of ZIKV complexed with Fab C10 | |||||||||
Sample |
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Keywords | antibody / neutralization / VIRUS | |||||||||
| Function / homology | Function and homology informationflavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / negative regulation of innate immune response / ribonucleoside triphosphate phosphatase activity / viral capsid / double-stranded RNA binding / nucleoside-triphosphate phosphatase / 4 iron, 4 sulfur cluster binding ...flavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / negative regulation of innate immune response / ribonucleoside triphosphate phosphatase activity / viral capsid / double-stranded RNA binding / nucleoside-triphosphate phosphatase / 4 iron, 4 sulfur cluster binding / clathrin-dependent endocytosis of virus by host cell / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / molecular adaptor activity / methyltransferase cap1 activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / protein dimerization activity / host cell perinuclear region of cytoplasm / symbiont-mediated suppression of host innate immune response / host cell endoplasmic reticulum membrane / RNA helicase / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont-mediated activation of host autophagy / RNA-directed RNA polymerase / serine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / fusion of virus membrane with host endosome membrane / viral envelope / lipid binding / centrosome / symbiont entry into host cell / GTP binding / virion attachment to host cell / host cell nucleus / virion membrane / structural molecule activity / ATP hydrolysis activity / proteolysis / extracellular region / ATP binding / metal ion binding / membrane Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) / ![]() Zika virus | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 9.4 Å | |||||||||
Authors | Morrone S / Chew SV | |||||||||
| Funding support | Singapore, 2 items
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Citation | Journal: Nat Commun / Year: 2020Title: High flavivirus structural plasticity demonstrated by a non-spherical morphological variant. Authors: Seamus R Morrone / Valerie S Y Chew / Xin-Ni Lim / Thiam-Seng Ng / Victor A Kostyuchenko / Shuijun Zhang / Melissa Wirawan / Pau-Ling Chew / Jaime Lee / Joanne L Tan / Jiaqi Wang / Ter Yong ...Authors: Seamus R Morrone / Valerie S Y Chew / Xin-Ni Lim / Thiam-Seng Ng / Victor A Kostyuchenko / Shuijun Zhang / Melissa Wirawan / Pau-Ling Chew / Jaime Lee / Joanne L Tan / Jiaqi Wang / Ter Yong Tan / Jian Shi / Gavin Screaton / Marc C Morais / Shee-Mei Lok / ![]() Abstract: Previous flavivirus (dengue and Zika viruses) studies showed largely spherical particles either with smooth or bumpy surfaces. Here, we demonstrate flavivirus particles have high structural ...Previous flavivirus (dengue and Zika viruses) studies showed largely spherical particles either with smooth or bumpy surfaces. Here, we demonstrate flavivirus particles have high structural plasticity by the induction of a non-spherical morphology at elevated temperatures: the club-shaped particle (clubSP), which contains a cylindrical tail and a disc-like head. Complex formation of DENV and ZIKV with Fab C10 stabilize the viruses allowing cryoEM structural determination to ~10 Å resolution. The caterpillar-shaped (catSP) Fab C10:ZIKV complex shows Fabs locking the E protein raft structure containing three E dimers. However, compared to the original spherical structure, the rafts have rotated relative to each other. The helical tail structure of Fab C10:DENV3 clubSP showed although the Fab locked an E protein dimer, the dimers have shifted laterally. Morphological diversity, including clubSP and the previously identified bumpy and smooth-surfaced spherical particles, may help flavivirus survival and immune evasion. | |||||||||
| History |
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Structure visualization
| Movie |
Movie viewer |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_30279.map.gz | 218.1 MB | EMDB map data format | |
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| Header (meta data) | emd-30279-v30.xml emd-30279.xml | 16.1 KB 16.1 KB | Display Display | EMDB header |
| Images | emd_30279.png | 110.7 KB | ||
| Filedesc metadata | emd-30279.cif.gz | 6.3 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-30279 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-30279 | HTTPS FTP |
-Validation report
| Summary document | emd_30279_validation.pdf.gz | 574.9 KB | Display | EMDB validaton report |
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| Full document | emd_30279_full_validation.pdf.gz | 574.5 KB | Display | |
| Data in XML | emd_30279_validation.xml.gz | 7.3 KB | Display | |
| Data in CIF | emd_30279_validation.cif.gz | 8.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30279 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30279 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7c2tMC ![]() 7c2sC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_30279.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | helical reconstruction of ZIKV complexed with Fab C10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.34 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Helical reconstruction of Zika virus complexed with Fab C10
| Entire | Name: Helical reconstruction of Zika virus complexed with Fab C10 |
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| Components |
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-Supramolecule #1: Helical reconstruction of Zika virus complexed with Fab C10
| Supramolecule | Name: Helical reconstruction of Zika virus complexed with Fab C10 type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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-Supramolecule #2: C10 Fab
| Supramolecule | Name: C10 Fab / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #3-#4 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Supramolecule #3: Zika virus H/PF/2013 strain
| Supramolecule | Name: Zika virus H/PF/2013 strain / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: ![]() Zika virus |
-Macromolecule #1: envelope protein
| Macromolecule | Name: envelope protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() Zika virus |
| Molecular weight | Theoretical: 54.444051 KDa |
| Sequence | String: IRCIGVSNRD FVEGMSGGTW VDVVLEHGGC VTVMAQDKPT VDIELVTTTV SNMAEVRSYC YEASISDMAS DSRCPTQGEA YLDKQSDTQ YVCKRTLVDR GWGNGCGLFG KGSLVTCAKF ACSKKMTGKS IQPENLEYRI MLSVHGSQHS GMIVNDTGHE T DENRAKVE ...String: IRCIGVSNRD FVEGMSGGTW VDVVLEHGGC VTVMAQDKPT VDIELVTTTV SNMAEVRSYC YEASISDMAS DSRCPTQGEA YLDKQSDTQ YVCKRTLVDR GWGNGCGLFG KGSLVTCAKF ACSKKMTGKS IQPENLEYRI MLSVHGSQHS GMIVNDTGHE T DENRAKVE ITPNSPRAEA TLGGFGSLGL DCEPRTGLDF SDLYYLTMNN KHWLVHKEWF HDIPLPWHAG ADTGTPHWNN KE ALVEFKD AHAKRQTVVV LGSQEGAVHT ALAGALEAEM DGAKGRLSSG HLKCRLKMDK LRLKGVSYSL CTAAFTFTKI PAE TLHGTV TVEVQYAGTD GPCKVPAQMA VDMQTLTPVG RLITANPVIT ESTENSKMML ELDPPFGDSY IVIGVGEKKI THHW HRSGS TIGKAFEATV RGAKRMAVLG DTAWDFGSVG GALNSLGKGI HQIFGAAFKS LFGGMSWFSQ ILIGTLLMWL GLNTK NGSI SLMCLALGGV LIFLSTAVSA UniProtKB: Genome polyprotein |
-Macromolecule #2: M protein
| Macromolecule | Name: M protein / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() Zika virus |
| Molecular weight | Theoretical: 8.496883 KDa |
| Sequence | String: AVTLPSHSTR KLQTRSQTWL ESREYTKHLI RVENWIFRNP GFALAAAAIA WLLGSSTSQK VIYLVMILLI APAYS UniProtKB: Genome polyprotein |
-Macromolecule #3: Heavy chain from Fab C10
| Macromolecule | Name: Heavy chain from Fab C10 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 14.487058 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: EVQLVESGAE VKKPGASVKV SCKASGYTFT SYAMHWVRQA PGQRLEWMGW INAGNGNTKY SQKFQDRVTI TRDTSASTAY MELSSLRSE DTAIYYCARD KVDDYGDYWF PTLWYFDYWG QGTLVTVS |
-Macromolecule #4: Light chain from Fab C10
| Macromolecule | Name: Light chain from Fab C10 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 11.298362 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: SALTQPASVS GSPGQSITIS CTGTSSDVGG FNYVSWFQQH PGKAPKLMLY DVTSRPSGVS SRFSGSKSGN TASLTISGLQ AEDEADYYC SSHTSRGTWV FGGGTKLTVL |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | helical reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 38.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Final reconstruction | Applied symmetry - Helical parameters - Δz: 8.6 Å Applied symmetry - Helical parameters - Δ&Phi: 24.1 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 9.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 3406 |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| Startup model | Type of model: EMDB MAP |
| Final angle assignment | Type: PROJECTION MATCHING |
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About Yorodumi



Keywords
Homo sapiens (human)
Zika virus
Authors
Singapore, 2 items
Citation

UCSF Chimera











Z (Sec.)
Y (Row.)
X (Col.)






















