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- EMDB-38383: Structure of Eastern Equine Encephalitis VLP PE6-K156A in complex... -

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Entry
Database: EMDB / ID: EMD-38383
TitleStructure of Eastern Equine Encephalitis VLP PE6-K156A in complex with the receptor VLDLR LA1-8
Map data
Sample
  • Complex: Structure of East Equine Encephalitis VLP PE6-K156A in complex with the receptor VLDLR LA1-8
KeywordsEast Equine Encephalitis virus / EEEV / receptor / glycoprotein / ApoER2 / VIRAL PROTEIN
Biological speciesEastern equine encephalitis virus
Methodsingle particle reconstruction / cryo EM / Resolution: 11.0 Å
AuthorsCao D / Ma B / Cao Z / Xu X / Zhang X / Xiang Y
Funding support China, 3 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China) China
National Natural Science Foundation of China (NSFC) China
Chinese Academy of Sciences China
CitationJournal: Nat Commun / Year: 2024
Title: The receptor VLDLR binds Eastern Equine Encephalitis virus through multiple distinct modes.
Authors: Duanfang Cao / Bingting Ma / Ziyi Cao / Xiaoyu Xu / Xinzheng Zhang / Ye Xiang /
Abstract: Eastern Equine Encephalitis virus (EEEV) is an alphavirus that can cause severe diseases in infected humans. The very low-density lipoprotein receptor (VLDLR) was recently identified as a receptor of ...Eastern Equine Encephalitis virus (EEEV) is an alphavirus that can cause severe diseases in infected humans. The very low-density lipoprotein receptor (VLDLR) was recently identified as a receptor of EEEV. Herein, we performed cryo-electron microscopy structural and biochemistry studies on the specific interactions between EEEV and VLDLR. Our results show that VLDLR binds EEEV at three different sites A, B and C through its membrane-distal LDLR class A (LA) repeats. Site A is located in the cleft in between the E1-E2 heterodimers. Site B is located near the connecting β ribbon of E2 and is in proximity to site A, while site C is on the domain B of E2. The binding of VLDLR LAs to EEEV is in complex modes, including the LA1-2 and LA3-5 mediated two major modes. Disruption of the LA1-2 mediated binding significantly affect the cell attachment of EEEV. However, the mutation W132G of VLDLR impairs the binding of LA3, drives the switch of the binding modes, and significantly enhances the attachment of EEEV to the cell. The W132G variant of VLDLR could be identified in human genome and SNP sequences, implying that people with similar mutations in VLDLR may be highly susceptible to EEEV infection.
History
DepositionDec 19, 2023-
Header (metadata) releaseAug 28, 2024-
Map releaseAug 28, 2024-
UpdateAug 28, 2024-
Current statusAug 28, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_38383.png

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Map

FileDownload / File: emd_38383.map.gz / Format: CCP4 / Size: 98.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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AxesZ (Sec.)Y (Row.)X (Col.)
1.33 Å/pix.
x 296 pix.
= 393.68 Å		1.33 Å/pix.
x 296 pix.
= 393.68 Å		1.33 Å/pix.
x 296 pix.
= 393.68 Å

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.33 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.005
Minimum - Maximum-0.011781366 - 0.019255731
Average (Standard dev.)0.00084811944 (±0.0027966204)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions296296296
Spacing296296296
CellA=B=C: 393.68002 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_38383_additional_1.map
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Half map: #1

Fileemd_38383_half_map_1.map
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Half map: #2

Fileemd_38383_half_map_2.map
Projections & Slices
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Sample components

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Entire : Structure of East Equine Encephalitis VLP PE6-K156A in complex wi...

EntireName: Structure of East Equine Encephalitis VLP PE6-K156A in complex with the receptor VLDLR LA1-8
Components
  • Complex: Structure of East Equine Encephalitis VLP PE6-K156A in complex with the receptor VLDLR LA1-8

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Supramolecule #1: Structure of East Equine Encephalitis VLP PE6-K156A in complex wi...

SupramoleculeName: Structure of East Equine Encephalitis VLP PE6-K156A in complex with the receptor VLDLR LA1-8
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Source (natural)Organism: Eastern equine encephalitis virus

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TECNAI ARCTICA
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.7 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 11.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 2905
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING

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