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- EMDB-35471: Semliki Forest virus VLP in complex with the receptor VLDLR LA2-3 -
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Open data
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Basic information
Entry | ![]() | ||||||||||||
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Title | Semliki Forest virus VLP in complex with the receptor VLDLR LA2-3 | ||||||||||||
![]() | Overall density map of SFV VLP in complex with VLDLR LA2-3 | ||||||||||||
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Biological species | ![]() ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.5 Å | ||||||||||||
![]() | Cao D / Ma B / Cao Z / Zhang X / Xiang Y | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of Semliki Forest virus in complex with its receptor VLDLR. Authors: Duanfang Cao / Bingting Ma / Ziyi Cao / Xinzheng Zhang / Ye Xiang / ![]() Abstract: Semliki Forest virus (SFV) is an alphavirus that uses the very-low-density lipoprotein receptor (VLDLR) as a receptor during infection of its vertebrate hosts and insect vectors. Herein, we used ...Semliki Forest virus (SFV) is an alphavirus that uses the very-low-density lipoprotein receptor (VLDLR) as a receptor during infection of its vertebrate hosts and insect vectors. Herein, we used cryoelectron microscopy to study the structure of SFV in complex with VLDLR. We found that VLDLR binds multiple E1-DIII sites of SFV through its membrane-distal LDLR class A (LA) repeats. Among the LA repeats of the VLDLR, LA3 has the best binding affinity to SFV. The high-resolution structure shows that LA3 binds SFV E1-DIII through a small surface area of 378 Å, with the main interactions at the interface involving salt bridges. Compared with the binding of single LA3s, consecutive LA repeats around LA3 promote synergistic binding to SFV, during which the LAs undergo a rotation, allowing simultaneous key interactions at multiple E1-DIII sites on the virion and enabling the binding of VLDLRs from divergent host species to SFV. | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 695.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16 KB 16 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 20.6 KB | Display | ![]() |
Images | ![]() | 178.1 KB | ||
Others | ![]() ![]() ![]() ![]() | 80.4 MB 45.4 MB 612.8 MB 612.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Annotation | Overall density map of SFV VLP in complex with VLDLR LA2-3 | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.35 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Density map of SFV VLP in complex with VLDLR LA2-3 at the 2-fold axis
File | emd_35471_additional_1.map | ||||||||||||
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Annotation | Density map of SFV VLP in complex with VLDLR LA2-3 at the 2-fold axis | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Density map of SFV VLP in complex with VLDLR LA2-3 at the 5-fold axis
File | emd_35471_additional_2.map | ||||||||||||
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Annotation | Density map of SFV VLP in complex with VLDLR LA2-3 at the 5-fold axis | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_35471_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_35471_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Semliki Forest virus VLP in complex with the receptor VLDLR LA2-3
Entire | Name: Semliki Forest virus VLP in complex with the receptor VLDLR LA2-3 |
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Components |
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-Supramolecule #1: Semliki Forest virus VLP in complex with the receptor VLDLR LA2-3
Supramolecule | Name: Semliki Forest virus VLP in complex with the receptor VLDLR LA2-3 type: complex / ID: 1 / Chimera: Yes / Parent: 0 |
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Source (natural) | Organism: ![]() ![]() |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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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: DIRECT ELECTRON DE-16 (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.7 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |