|Entry||Database: PDB / ID: 6akt|
|Title||Cryo-EM structure of CVA10 A-particle|
|Keywords||VIRUS / picornavirus uncoating / receptor binding|
|Function / homology||Peptidase C3, picornavirus core protein 2A / picornavirus capsid protein / Helicase, superfamily 3, single-stranded RNA virus / Peptidase S1, PA clan / RNA-directed RNA polymerase, catalytic domain / AAA+ ATPase domain / Picornavirus coat protein VP4 / Picornavirus 2B protein / Picornavirus capsid / RNA-directed RNA polymerase, C-terminal domain ...Peptidase C3, picornavirus core protein 2A / picornavirus capsid protein / Helicase, superfamily 3, single-stranded RNA virus / Peptidase S1, PA clan / RNA-directed RNA polymerase, catalytic domain / AAA+ ATPase domain / Picornavirus coat protein VP4 / Picornavirus 2B protein / Picornavirus capsid / RNA-directed RNA polymerase, C-terminal domain / Helicase, superfamily 3, single-stranded DNA/RNA virus / Peptidase C3A/C3B, picornaviral / Viral coat protein subunit / Picornavirus/Calicivirus coat protein / P-loop containing nucleoside triphosphate hydrolase / Poliovirus core protein 3a, soluble domain / 3C cysteine protease (picornain 3C) / RNA dependent RNA polymerase / Superfamily 3 helicase of positive ssRNA viruses domain profile. / RdRp of positive ssRNA viruses catalytic domain profile. / Poliovirus 3A protein like / Picornavirus coat protein (VP4) / Picornavirus 2B protein / Picornavirus core protein 2A / RNA helicase / Poliovirus 3A protein-like / T=pseudo3 icosahedral viral capsid / picornain 2A / pore-mediated entry of viral genome into host cell / suppression by virus of host mRNA export from nucleus / suppression by virus of host RIG-I activity / picornain 3C / endocytosis involved in viral entry into host cell / RNA-protein covalent cross-linking / host cell cytoplasmic vesicle membrane / pore formation by virus in membrane of host cell / integral to membrane of host cell / RNA helicase activity / nucleoside-triphosphate phosphatase / viral capsid / RNA-directed RNA polymerase / suppression by virus of host gene expression / induction by virus of host autophagy / ion channel activity / protein complex oligomerization / viral RNA genome replication / RNA-directed 5'-3' RNA polymerase activity / cysteine-type endopeptidase activity / transcription, DNA-templated / virion attachment to host cell / structural molecule activity / RNA binding / membrane / ATP binding / Genome polyprotein / Genome polyprotein / VP1|
Function and homology information
|Specimen source||Coxsackievirus A10|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 2.8 Å resolution|
|Authors||Zhu, L. / Sun, Y. / Fan, J.Y. / Zhu, B. / Cao, L. / Gao, Q. / Zhang, Y.J. / Liu, H.R. / Rao, Z.H. / Wang, X.X.|
|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
SummaryFull reportAbout validation report
|Date||Deposition: Sep 3, 2018 / Release: Jan 16, 2019|
|Structure viewer||Molecule: |
Downloads & links
A: VP1x 60
A: VP1x 5
A: VP1x 6
|#1: Protein/peptide|| |
Mass: 33232.383 Da / Num. of mol.: 1 / Source: (gene. exp.) Coxsackievirus A10 / Production host: Chlorocebus aethiops (grivet) / References: UniProt: W0G0K3
|#2: Protein/peptide|| |
Mass: 27783.105 Da / Num. of mol.: 1 / Source: (gene. exp.) Coxsackievirus A10 / Production host: Chlorocebus aethiops (grivet) / References: UniProt: A0A0C5AZ80
|#3: Protein/peptide|| |
Mass: 26279.826 Da / Num. of mol.: 1 / Source: (gene. exp.) Coxsackievirus A10 / Production host: Chlorocebus aethiops (grivet) / References: UniProt: A0A0C5AWF6
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: single particle reconstruction|
|Component||Name: Coxsackievirus A10 / Type: VIRUS / Entity ID: 1,||Source (natural)||Organism: Coxsackievirus A10||Source (recombinant)||Organism: Chlorocebus aethiops (grivet)||Details of virus||Empty: NO / Enveloped: NO / Virus isolate: SEROTYPE / Virus type: VIRION||Buffer solution||pH: 7.4||Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES||Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 25 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|Software||Name: PHENIX / Version: 1.10.1_2155: / Classification: refinement|
|CTF correction||Type: NONE|
|3D reconstruction||Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 21456 / Symmetry type: POINT|
|Refine LS restraints|
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