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- PDB-7fj3: Cryo-EM structure of PRV A-capid -

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Basic information

Entry
Database: PDB / ID: 7fj3
TitleCryo-EM structure of PRV A-capid
Components
  • Major capsid protein
  • Small capsomere-interacting protein
  • Triplex capsid protein 1
  • Triplex capsid protein 2
KeywordsVIRUS / Pseudorabies virus / C-capsid / Cryo-EM
Function / homology
Function and homology information


T=16 icosahedral viral capsid / viral capsid assembly / viral process / viral capsid / host cell nucleus / structural molecule activity / DNA binding
Similarity search - Function
Herpesvirus UL35 / Herpesvirus UL35 family / Herpesvirus capsid protein 2 / Herpesvirus capsid shell protein 1 / Herpesvirus VP23 like capsid protein / Herpesvirus capsid shell protein VP19C / Herpesvirus major capsid protein / Herpesvirus major capsid protein, upper domain superfamily / Herpes virus major capsid protein
Similarity search - Domain/homology
Small capsomere-interacting protein / Major capsid protein / Triplex capsid protein 2 / Triplex capsid protein 1
Similarity search - Component
Biological speciesSuid alphaherpesvirus 1
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.53 Å
AuthorsZheng, Q. / Li, S. / Zha, Z. / Sun, H.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nat Commun / Year: 2022
Title: Structures of pseudorabies virus capsids.
Authors: Guosong Wang / Zhenghui Zha / Pengfei Huang / Hui Sun / Yang Huang / Maozhou He / Tian Chen / Lina Lin / Zhenqin Chen / Zhibo Kong / Yuqiong Que / Tingting Li / Ying Gu / Hai Yu / Jun Zhang ...Authors: Guosong Wang / Zhenghui Zha / Pengfei Huang / Hui Sun / Yang Huang / Maozhou He / Tian Chen / Lina Lin / Zhenqin Chen / Zhibo Kong / Yuqiong Que / Tingting Li / Ying Gu / Hai Yu / Jun Zhang / Qingbing Zheng / Yixin Chen / Shaowei Li / Ningshao Xia /
Abstract: Pseudorabies virus (PRV) is a major etiological agent of swine infectious diseases and is responsible for significant economic losses in the swine industry. Recent data points to human viral ...Pseudorabies virus (PRV) is a major etiological agent of swine infectious diseases and is responsible for significant economic losses in the swine industry. Recent data points to human viral encephalitis caused by PRV infection, suggesting that PRV may be able to overcome the species barrier to infect humans. To date, there is no available therapeutic for PRV infection. Here, we report the near-atomic structures of the PRV A-capsid and C-capsid, and illustrate the interaction that occurs between these subunits. We show that the C-capsid portal complex is decorated with capsid-associated tegument complexes. The PRV capsid structure is highly reminiscent of other α-herpesviruses, with some additional structural features of β- and γ-herpesviruses. These results illustrate the structure of the PRV capsid and elucidate the underlying assembly mechanism at the molecular level. This knowledge may be useful for the development of oncolytic agents or specific therapeutics against this arm of the herpesvirus family.
History
DepositionAug 2, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 22, 2022Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
0: Major capsid protein
1: Triplex capsid protein 2
2: Triplex capsid protein 2
3: Triplex capsid protein 2
A: Major capsid protein
B: Triplex capsid protein 1
C: Triplex capsid protein 1
D: Triplex capsid protein 1
E: Small capsomere-interacting protein
F: Small capsomere-interacting protein
G: Small capsomere-interacting protein
H: Small capsomere-interacting protein
I: Small capsomere-interacting protein
J: Small capsomere-interacting protein
K: Small capsomere-interacting protein
L: Small capsomere-interacting protein
M: Small capsomere-interacting protein
N: Small capsomere-interacting protein
O: Small capsomere-interacting protein
P: Small capsomere-interacting protein
Q: Small capsomere-interacting protein
R: Small capsomere-interacting protein
S: Major capsid protein
T: Triplex capsid protein 1
U: Major capsid protein
V: Small capsomere-interacting protein
W: Triplex capsid protein 1
a: Major capsid protein
d: Triplex capsid protein 1
e: Major capsid protein
f: Major capsid protein
g: Major capsid protein
h: Triplex capsid protein 1
i: Triplex capsid protein 1
j: Triplex capsid protein 2
k: Triplex capsid protein 2
l: Major capsid protein
m: Major capsid protein
n: Major capsid protein
o: Triplex capsid protein 2
p: Major capsid protein
q: Major capsid protein
r: Triplex capsid protein 1
s: Triplex capsid protein 2
t: Triplex capsid protein 1
u: Major capsid protein
v: Triplex capsid protein 2
w: Major capsid protein
x: Triplex capsid protein 2
y: Major capsid protein
z: Triplex capsid protein 2


Theoretical massNumber of molelcules
Total (without water)3,227,99351
Polymers3,227,99351
Non-polymers00
Water0
1
0: Major capsid protein
1: Triplex capsid protein 2
2: Triplex capsid protein 2
3: Triplex capsid protein 2
A: Major capsid protein
B: Triplex capsid protein 1
C: Triplex capsid protein 1
D: Triplex capsid protein 1
E: Small capsomere-interacting protein
F: Small capsomere-interacting protein
G: Small capsomere-interacting protein
H: Small capsomere-interacting protein
I: Small capsomere-interacting protein
J: Small capsomere-interacting protein
K: Small capsomere-interacting protein
L: Small capsomere-interacting protein
M: Small capsomere-interacting protein
N: Small capsomere-interacting protein
O: Small capsomere-interacting protein
P: Small capsomere-interacting protein
Q: Small capsomere-interacting protein
R: Small capsomere-interacting protein
S: Major capsid protein
T: Triplex capsid protein 1
U: Major capsid protein
V: Small capsomere-interacting protein
W: Triplex capsid protein 1
a: Major capsid protein
d: Triplex capsid protein 1
e: Major capsid protein
f: Major capsid protein
g: Major capsid protein
h: Triplex capsid protein 1
i: Triplex capsid protein 1
j: Triplex capsid protein 2
k: Triplex capsid protein 2
l: Major capsid protein
m: Major capsid protein
n: Major capsid protein
o: Triplex capsid protein 2
p: Major capsid protein
q: Major capsid protein
r: Triplex capsid protein 1
s: Triplex capsid protein 2
t: Triplex capsid protein 1
u: Major capsid protein
v: Triplex capsid protein 2
w: Major capsid protein
x: Triplex capsid protein 2
y: Major capsid protein
z: Triplex capsid protein 2
x 60


  • complete icosahedral assembly
  • Evidence: electron microscopy
  • 194 MDa, 3060 polymers
Theoretical massNumber of molelcules
Total (without water)193,679,6093060
Polymers193,679,6093060
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation59
2


  • Idetical with deposited unit
  • icosahedral asymmetric unit
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
0: Major capsid protein
1: Triplex capsid protein 2
2: Triplex capsid protein 2
3: Triplex capsid protein 2
A: Major capsid protein
B: Triplex capsid protein 1
C: Triplex capsid protein 1
D: Triplex capsid protein 1
E: Small capsomere-interacting protein
F: Small capsomere-interacting protein
G: Small capsomere-interacting protein
H: Small capsomere-interacting protein
I: Small capsomere-interacting protein
J: Small capsomere-interacting protein
K: Small capsomere-interacting protein
L: Small capsomere-interacting protein
M: Small capsomere-interacting protein
N: Small capsomere-interacting protein
O: Small capsomere-interacting protein
P: Small capsomere-interacting protein
Q: Small capsomere-interacting protein
R: Small capsomere-interacting protein
S: Major capsid protein
T: Triplex capsid protein 1
U: Major capsid protein
V: Small capsomere-interacting protein
W: Triplex capsid protein 1
a: Major capsid protein
d: Triplex capsid protein 1
e: Major capsid protein
f: Major capsid protein
g: Major capsid protein
h: Triplex capsid protein 1
i: Triplex capsid protein 1
j: Triplex capsid protein 2
k: Triplex capsid protein 2
l: Major capsid protein
m: Major capsid protein
n: Major capsid protein
o: Triplex capsid protein 2
p: Major capsid protein
q: Major capsid protein
r: Triplex capsid protein 1
s: Triplex capsid protein 2
t: Triplex capsid protein 1
u: Major capsid protein
v: Triplex capsid protein 2
w: Major capsid protein
x: Triplex capsid protein 2
y: Major capsid protein
z: Triplex capsid protein 2
x 5


  • icosahedral pentamer
  • 16.1 MDa, 255 polymers
Theoretical massNumber of molelcules
Total (without water)16,139,967255
Polymers16,139,967255
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
4
0: Major capsid protein
1: Triplex capsid protein 2
2: Triplex capsid protein 2
3: Triplex capsid protein 2
A: Major capsid protein
B: Triplex capsid protein 1
C: Triplex capsid protein 1
D: Triplex capsid protein 1
E: Small capsomere-interacting protein
F: Small capsomere-interacting protein
G: Small capsomere-interacting protein
H: Small capsomere-interacting protein
I: Small capsomere-interacting protein
J: Small capsomere-interacting protein
K: Small capsomere-interacting protein
L: Small capsomere-interacting protein
M: Small capsomere-interacting protein
N: Small capsomere-interacting protein
O: Small capsomere-interacting protein
P: Small capsomere-interacting protein
Q: Small capsomere-interacting protein
R: Small capsomere-interacting protein
S: Major capsid protein
T: Triplex capsid protein 1
U: Major capsid protein
V: Small capsomere-interacting protein
W: Triplex capsid protein 1
a: Major capsid protein
d: Triplex capsid protein 1
e: Major capsid protein
f: Major capsid protein
g: Major capsid protein
h: Triplex capsid protein 1
i: Triplex capsid protein 1
j: Triplex capsid protein 2
k: Triplex capsid protein 2
l: Major capsid protein
m: Major capsid protein
n: Major capsid protein
o: Triplex capsid protein 2
p: Major capsid protein
q: Major capsid protein
r: Triplex capsid protein 1
s: Triplex capsid protein 2
t: Triplex capsid protein 1
u: Major capsid protein
v: Triplex capsid protein 2
w: Major capsid protein
x: Triplex capsid protein 2
y: Major capsid protein
z: Triplex capsid protein 2
x 6


  • icosahedral 23 hexamer
  • 19.4 MDa, 306 polymers
Theoretical massNumber of molelcules
Total (without water)19,367,961306
Polymers19,367,961306
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation5
5


  • Idetical with deposited unit in distinct coordinate
  • icosahedral asymmetric unit, std point frame
TypeNameSymmetry operationNumber
transform to point frame1
SymmetryPoint symmetry: (Schoenflies symbol: I (icosahedral))

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Components

#1: Protein
Major capsid protein / MCP


Mass: 146101.984 Da / Num. of mol.: 16 / Source method: isolated from a natural source / Source: (natural) Suid alphaherpesvirus 1 / References: UniProt: G3G8T2
#2: Protein
Triplex capsid protein 2


Mass: 31763.766 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) Suid alphaherpesvirus 1 / References: UniProt: G3G8T3
#3: Protein
Triplex capsid protein 1


Mass: 40008.594 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) Suid alphaherpesvirus 1 / References: UniProt: Q85211
#4: Protein
Small capsomere-interacting protein


Mass: 11509.209 Da / Num. of mol.: 15 / Source method: isolated from a natural source / Source: (natural) Suid alphaherpesvirus 1 / References: UniProt: G3G8R4

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Cryo-EM structure of PRV A-capsid / Type: VIRUS / Entity ID: all / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Suid alphaherpesvirus 1
Details of virusEmpty: NO / Enveloped: YES / Isolate: OTHER / Type: VIRION
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Tecnai F30 / Image courtesy: FEI Company
MicroscopyModel: FEI TECNAI F30
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingElectron dose: 60 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k)

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Processing

SoftwareName: UCSF ChimeraX / Version: 1.3/v9 / Classification: model building / URL: https://www.rbvi.ucsf.edu/chimerax/ / Os: Linux / Type: package
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4.53 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 8899 / Symmetry type: POINT

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