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- EMDB-37420: CryoEM structure of non-structural protein 1 tetramer from dengue... -
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Open data
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Basic information
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Title | CryoEM structure of non-structural protein 1 tetramer from dengue virus type 4 | |||||||||
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Function / homology | ![]() symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Jiao HZ / Pan Q / Hu HL | |||||||||
Funding support | 1 items
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![]() | ![]() Title: The step-by-step assembly mechanism of secreted flavivirus NS1 tetramer and hexamer captured at atomic resolution. Authors: Qi Pan / Haizhan Jiao / Wanqin Zhang / Qiang Chen / Geshu Zhang / Jianhai Yu / Wei Zhao / Hongli Hu / ![]() Abstract: Flaviviruses encode a conserved, membrane-associated nonstructural protein 1 (NS1) with replication and immune evasion functions. The current knowledge of secreted NS1 (sNS1) oligomers is based on ...Flaviviruses encode a conserved, membrane-associated nonstructural protein 1 (NS1) with replication and immune evasion functions. The current knowledge of secreted NS1 (sNS1) oligomers is based on several low-resolution structures, thus hindering the development of drugs and vaccines against flaviviruses. Here, we revealed that recombinant sNS1 from flaviviruses exists in a dynamic equilibrium of dimer-tetramer-hexamer states. Two DENV4 hexameric NS1 structures and several tetrameric NS1 structures from multiple flaviviruses were solved at atomic resolution by cryo-EM. The stacking of the tetrameric NS1 and hexameric NS1 is facilitated by the hydrophobic β-roll and connector domains. Additionally, a triacylglycerol molecule located within the central cavity may play a role in stabilizing the hexamer. Based on differentiated interactions between the dimeric NS1, two distinct hexamer models (head-to-head and side-to-side hexamer) and the step-by-step assembly mechanisms of NS1 dimer into hexamer were proposed. We believe that our study sheds light on the understanding of the NS1 oligomerization and contributes to NS1-based therapies. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 79 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.7 KB 15.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.2 KB | Display | ![]() |
Images | ![]() | 157.7 KB | ||
Filedesc metadata | ![]() | 5.4 KB | ||
Others | ![]() ![]() ![]() | 42 MB 77.6 MB 77.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8wbcMC ![]() 8wbbC ![]() 8wbdC ![]() 8wbeC ![]() 8wbfC ![]() 8wbgC ![]() 8wbhC 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: 0.85 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: #1
File | emd_37420_additional_1.map | ||||||||||||
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Density Histograms |
-Half map: #1
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Density Histograms |
-Half map: #2
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Density Histograms |
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Sample components
-Entire : dengue virus type 4 non-structural protein 1 tetramer
Entire | Name: dengue virus type 4 non-structural protein 1 tetramer |
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Components |
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-Supramolecule #1: dengue virus type 4 non-structural protein 1 tetramer
Supramolecule | Name: dengue virus type 4 non-structural protein 1 tetramer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Genome polyprotein
Macromolecule | Name: Genome polyprotein / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 40.494758 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: DTGCAVSWSG KELKCGSGIF VIDNVHTWTE QYKFQPESPA RLASAILNAH EDGVCGIRST TRLENIMWKQ ITNELNYVLW EGGHDLTVV AGDVKGVLSK GKRALAPPVN DLKYSWKTWG KAKIFTPEAK NSTFLIDGPD TSECPNERRA WNFLEVEDYG F GMFTTNIW ...String: DTGCAVSWSG KELKCGSGIF VIDNVHTWTE QYKFQPESPA RLASAILNAH EDGVCGIRST TRLENIMWKQ ITNELNYVLW EGGHDLTVV AGDVKGVLSK GKRALAPPVN DLKYSWKTWG KAKIFTPEAK NSTFLIDGPD TSECPNERRA WNFLEVEDYG F GMFTTNIW MKFREGSSEV CDHRLMSAAI KDQKAVHADM GYWIESSKNQ TWQIEKASLI EVKTCLWPKT HTLWSNGVLE SQ MLIPKAY AGPFSQHNYR QGYATQTVGP WHLGKLEIDF GECPGTTVTI QEDCDHRGPS LRTTTASGKL VTQWCCRSCT MPP LRFLGE DGCWYGMEIR PLSEKEENMV KSQVSAHHHH HH UniProtKB: Genome polyprotein |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 54.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |