[English] 日本語
Yorodumi
- PDB-9n5m: The Turkey Parvovirus Capsid structure -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9n5m
TitleThe Turkey Parvovirus Capsid structure
ComponentsVP2
KeywordsVIRUS / Capsid / Aveparvovirus / Turkey Parvovirus / cryo-EM / TuPV
Function / homologyParvovirus coat protein VP2 / Parvovirus coat protein VP1/VP2 / Parvovirus coat protein VP2 / Capsid/spike protein, ssDNA virus / T=1 icosahedral viral capsid / structural molecule activity / VP2
Function and homology information
Biological speciesTurkey parvovirus 260
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.35 Å
AuthorsHsi, J. / Mietzsch, M. / McKenna, R.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM082946 United States
National Science Foundation (NSF, United States)DGE-2236414 United States
CitationJournal: J Virol / Year: 2025
Title: Birds of a feather flock together: structural characterization of red-crowned crane and turkey aveparvoviruses.
Authors: Jane Hsi / Mario Mietzsch / Matthew Patney / Sunny Chen / Anjelique Sawh-Gopal / Paul Chipman / Robert McKenna /
Abstract: The parvoviruses have non-enveloped = 1 icosahedral capsids that are ~25 nm in diameter, which package linear single-stranded DNA and infect a wide range of hosts. To date, parvoviruses affecting ...The parvoviruses have non-enveloped = 1 icosahedral capsids that are ~25 nm in diameter, which package linear single-stranded DNA and infect a wide range of hosts. To date, parvoviruses affecting birds have been identified in two genera: - and , and no capsid structures have been determined for any member of . This study investigates two bird viruses of this genus: red-crowned crane parvovirus (RCPV) and turkey parvovirus (TuPV). While the pathogenicity of RCPV is currently unknown, TuPV has been associated with gastrointestinal diseases, especially in juvenile birds. High-resolution structures of the RCPV and TuPV capsids were determined by cryo-electron microscopy at a resolution of 2.66 Å and 2.35 Å, respectively. A structural comparison of the RCPV and TuPV capsids shows that they exhibit many conserved features, such as a channel at the five-fold symmetry axis and surface depressions at the two-fold axis, as previously observed in parvoviruses from other genera. However, major structural differences were observed at the three-fold axes, with both RCPV and TuPV displaying recessed protrusions. In addition, terminal sialic acid was identified as a potential glycan receptor for RCPV. This study extends the architectural portfolio of structural parvovirology and will provide insights into parvoviral diversity and characterization of these viruses.IMPORTANCEThis study presents the capsid structures of two aveparvoviruses, red-crowned crane parvovirus (RCPV) and turkey parvovirus (TuPV), extending the structural repertoire of the . While the pathogenicity of RCPV is unknown, the red-crowned cranes are among the rarest crane species. To date, very few virological studies have been conducted for this rare avian species, and understanding their virome could contribute to conservation efforts. Additionally, several studies have previously suggested that TuPV is associated with cases of enteric disease syndrome. To date, no commercial antivirals or vaccines are available for TuPV. The structural characterization of its capsid may contribute toward the development of a treatment to control the spread of infection.
History
DepositionFeb 4, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 2, 2025Provider: repository / Type: Initial release
Revision 1.0Jul 2, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jul 2, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 2, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 2, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jul 2, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Jul 16, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _em_admin.last_update
Revision 1.2Jul 30, 2025Group: Data collection / Database references / Category: citation / em_admin / Item: _citation.journal_volume / _em_admin.last_update

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: VP2
B: VP2
C: VP2
D: VP2
E: VP2
F: VP2
G: VP2
H: VP2
I: VP2
J: VP2
K: VP2
L: VP2
M: VP2
N: VP2
O: VP2
P: VP2
Q: VP2
R: VP2
S: VP2
T: VP2
U: VP2
V: VP2
W: VP2
X: VP2
Y: VP2
Z: VP2
a: VP2
b: VP2
c: VP2
d: VP2
e: VP2
f: VP2
g: VP2
h: VP2
i: VP2
j: VP2
k: VP2
l: VP2
m: VP2
n: VP2
o: VP2
p: VP2
q: VP2
r: VP2
s: VP2
t: VP2
u: VP2
v: VP2
w: VP2
x: VP2
y: VP2
z: VP2
1: VP2
2: VP2
3: VP2
4: VP2
5: VP2
6: VP2
7: VP2
8: VP2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)3,628,528180
Polymers3,625,61160
Non-polymers2,917120
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

-
Components

#1: Protein ...
VP2


Mass: 60426.852 Da / Num. of mol.: 60
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Turkey parvovirus 260 / Gene: VP2 / Cell line (production host): Sf9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: D3X6X8
#2: Chemical...
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 120 / Source method: obtained synthetically / Formula: Mg
Has ligand of interestN
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

ComponentName: Turkey parvovirus 260 / Type: VIRUS / Entity ID: #1 / Source: RECOMBINANT
Source (natural)Organism: Turkey parvovirus 260
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm) / Cell: Sf9
Details of virusEmpty: YES / Enveloped: NO / Isolate: SPECIES / Type: VIRUS-LIKE PARTICLE
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

-
Electron microscopy imaging

MicroscopyModel: JEOL CRYO ARM 300
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1990 nm / Nominal defocus min: 950 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

-
Processing

EM softwareName: PHENIX / Version: 1.10-2155_2155 / Category: model refinement
CTF correctionType: NONE
3D reconstructionResolution: 2.35 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 35131 / Symmetry type: POINT
RefinementStereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.011251160
ELECTRON MICROSCOPYf_angle_d0.858343020
ELECTRON MICROSCOPYf_dihedral_angle_d10.186200280
ELECTRON MICROSCOPYf_chiral_restr0.05735700
ELECTRON MICROSCOPYf_plane_restr0.00645000

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more