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- PDB-6m6i: Structure of HSV2 B-capsid portal vertex -

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Basic information

Entry
Database: PDB / ID: 6m6i
TitleStructure of HSV2 B-capsid portal vertex
Components
  • (Coiled coils chain ...) x 2
  • (Triplex capsid protein ...) x 2
  • Major capsid protein
  • Small capsomere-interacting protein
KeywordsVIRAL PROTEIN / HSV2 / Portal vertex / Complex
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
Capsid triplex subunit 2 / Small capsomere-interacting protein / Capsid triplex subunit 1 / Major capsid protein
Similarity search - Component
Biological speciesHuman herpesvirus 2
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.05 Å
AuthorsWang, X.X. / Wang, N.
CitationJournal: Protein Cell / Year: 2020
Title: Structures of the portal vertex reveal essential protein-protein interactions for Herpesvirus assembly and maturation.
Authors: Nan Wang / Wenyuan Chen / Ling Zhu / Dongjie Zhu / Rui Feng / Jialing Wang / Bin Zhu / Xinzheng Zhang / Xiaoqing Chen / Xianjie Liu / Runbin Yan / Dongyao Ni / Grace Guoying Zhou / Hongrong ...Authors: Nan Wang / Wenyuan Chen / Ling Zhu / Dongjie Zhu / Rui Feng / Jialing Wang / Bin Zhu / Xinzheng Zhang / Xiaoqing Chen / Xianjie Liu / Runbin Yan / Dongyao Ni / Grace Guoying Zhou / Hongrong Liu / Zihe Rao / Xiangxi Wang /
History
DepositionMar 14, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 10, 2021Provider: repository / Type: Initial release

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Structure viewerMolecule:
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Assembly

Deposited unit
A: Major capsid protein
B: Major capsid protein
C: Major capsid protein
D: Major capsid protein
E: Major capsid protein
F: Major capsid protein
G: Coiled coils chain 1
H: Coiled coils chain 2
I: Triplex capsid protein 2
J: Triplex capsid protein 2
K: Triplex capsid protein 1
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


Theoretical massNumber of molelcules
Total (without water)1,102,59017
Polymers1,102,59017
Non-polymers00
Water0
1
A: Major capsid protein
B: Major capsid protein
C: Major capsid protein
D: Major capsid protein
E: Major capsid protein
F: Major capsid protein
G: Coiled coils chain 1
H: Coiled coils chain 2
I: Triplex capsid protein 2
J: Triplex capsid protein 2
K: Triplex capsid protein 1
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
x 5


Theoretical massNumber of molelcules
Total (without water)5,512,94985
Polymers5,512,94985
Non-polymers00
Water0
TypeNameSymmetry operationNumber
point symmetry operation5
2


  • Idetical with deposited unit in distinct coordinate
  • point asymmetric unit
  • Evidence: microscopy
TypeNameSymmetry operationNumber
point symmetry operation1
3


  • Idetical with deposited unit in distinct coordinate
  • point asymmetric unit, std point frame
TypeNameSymmetry operationNumber
transform to point frame1
SymmetryPoint symmetry: (Schoenflies symbol: C5 (5 fold cyclic))

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Components

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Protein , 2 types, 12 molecules ABCDEFLMNOPQ

#1: Protein
Major capsid protein / MCP


Mass: 149399.359 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Human herpesvirus 2 / References: UniProt: P89442
#6: Protein
Small capsomere-interacting protein / VP26


Mass: 12147.707 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Human herpesvirus 2 / References: UniProt: G9I257

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Coiled coils chain ... , 2 types, 2 molecules GH

#2: Protein Coiled coils chain 1


Mass: 6911.511 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human herpesvirus 2
#3: Protein Coiled coils chain 2


Mass: 7081.720 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human herpesvirus 2

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Triplex capsid protein ... , 2 types, 3 molecules IJK

#4: Protein Triplex capsid protein 2 / VP23


Mass: 34373.785 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Human herpesvirus 2 / References: UniProt: G9I239
#5: Protein Triplex capsid protein 1 / VP19


Mass: 50566.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human herpesvirus 2 / References: UniProt: G9I260

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Details

Sequence detailsSequence for Coiled coils chains could not be identified.

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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: Human alphaherpesvirus 2 / Type: VIRUS / Entity ID: all / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Human alphaherpesvirus 2
Details of virusEmpty: NO / Enveloped: YES / Isolate: SPECIES / 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: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: DARK FIELD
Image recording
IDImaging-IDElectron dose (e/Å2)Film or detector model
1130FEI FALCON II (4k x 4k)
2130FEI FALCON II (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4.05 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 22158 / Symmetry type: POINT

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