|Entry||Database: EMDB / ID: EMD-9652|
|Title||Asymmetrical reconstruction of CVA10 A-particle|
|Function / homology|
Function and homology information
suppression by virus of host MDA-5 activity / picornain 2A / pore-mediated entry of viral genome into host cell / suppression by virus of host mRNA export from nucleus / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / RNA-protein covalent cross-linking / integral to membrane of host cell / pore formation by virus in membrane of host cell ...suppression by virus of host MDA-5 activity / picornain 2A / pore-mediated entry of viral genome into host cell / suppression by virus of host mRNA export from nucleus / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / RNA-protein covalent cross-linking / integral to membrane of host cell / pore formation by virus in membrane of host cell / viral capsid / protein complex oligomerization / cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / nucleoside-triphosphate phosphatase / suppression by virus of host gene expression / ion channel activity / induction by virus of host autophagy / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed 5'-3' RNA polymerase activity / RNA helicase activity / viral entry into host cell / transcription, DNA-templated / virion attachment to host cell / host cell nucleus / structural molecule activity / RNA binding / ATP binding / metal ion binding
Poliovirus 3A protein-like / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Picornavirus capsid / RNA-directed RNA polymerase, C-terminal domain / Helicase, superfamily 3, single-stranded DNA/RNA virus / Peptidase C3A/C3B, picornaviral / Peptidase C3, picornavirus core protein 2A / Viral coat protein subunit / Picornavirus/Calicivirus coat protein ...Poliovirus 3A protein-like / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Picornavirus capsid / RNA-directed RNA polymerase, C-terminal domain / Helicase, superfamily 3, single-stranded DNA/RNA virus / Peptidase C3A/C3B, picornaviral / Peptidase C3, picornavirus core protein 2A / Viral coat protein subunit / Picornavirus/Calicivirus coat protein / P-loop containing nucleoside triphosphate hydrolase / AAA+ ATPase domain / Picornavirus coat protein VP4 / Peptidase S1, PA clan, chymotrypsin-like fold / Picornavirales 3C/3C-like protease domain / Reverse transcriptase/Diguanylate cyclase domain / Helicase, superfamily 3, single-stranded RNA virus / DNA/RNA polymerase superfamily / Peptidase S1, PA clan / RNA-directed RNA polymerase, catalytic domain
Genome polyprotein / Genome polyprotein / Genome polyprotein
|Biological species||Coxsackievirus A10|
|Method||single particle reconstruction / cryo EM / Resolution: 12 Å|
|Authors||Zhu L / Sun Y / Rao ZH / Wang XX|
|Citation||Journal: Nat Commun / Year: 2018|
Title: Structures of Coxsackievirus A10 unveil the molecular mechanisms of receptor binding and viral uncoating.
Authors: Ling Zhu / Yao Sun / Jinyan Fan / Bin Zhu / Lei Cao / Qiang Gao / Yanjun Zhang / Hongrong Liu / Zihe Rao / Xiangxi Wang /
Abstract: Coxsackievirus A10 (CVA10), a human type-A Enterovirus (HEV-A), can cause diseases ranging from hand-foot-and-mouth disease to polio-myelitis-like disease. CVA10, together with some other HEV-As, ...Coxsackievirus A10 (CVA10), a human type-A Enterovirus (HEV-A), can cause diseases ranging from hand-foot-and-mouth disease to polio-myelitis-like disease. CVA10, together with some other HEV-As, utilizing the molecule KREMEN1 as an entry receptor, constitutes a KREMEN1-dependent subgroup within HEV-As. Currently, there is no vaccine or antiviral therapy available for treating diseases caused by CVA10. The atomic-resolution structure of the CVA10 virion, which is within the KREMEN1-dependent subgroup, shows significant conformational differences in the putative receptor binding sites and serotype-specific epitopes, when compared to the SCARB2-dependent subgroup of HEV-A, such as EV71, highlighting specific differences between the sub-groups. We also report two expanded structures of CVA10, an empty particle and uncoating intermediate at atomic resolution, as well as a medium-resolution genome structure reconstructed using a symmetry-mismatch method. Structural comparisons coupled with previous results, reveal an ordered signal transmission process for enterovirus uncoating, converting exo-genetic receptor-attachment inputs into a generic RNA release mechanism.
|Validation Report||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_9652.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.35 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Coxsackievirus A10
|Entire||Name: Coxsackievirus A10 / Number of components: 1|
-Component #1: virus, Coxsackievirus A10
|Virus||Name: Coxsackievirus A10 / Class: VIRION / Empty: No / Enveloped: No / Isolate: SEROTYPE|
|Species||Species: Coxsackievirus A10|
|Source (engineered)||Expression System: Chlorocebus aethiops (grivet)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 7.4|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 25 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 6500|
|3D reconstruction||Resolution: 12 Å / Resolution method: FSC 0.143 CUT-OFF|
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