[English] 日本語
Yorodumi
- PDB-7yfz: Cyanophage Pam3 baseplate proteins -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7yfz
TitleCyanophage Pam3 baseplate proteins
Components
  • (Pam3 baseplate wedge ...) x 2
  • Pam3 hub gp19
  • Pam3 plug gp18
  • Pam3 sheath initiator gp21
  • Pam3 spike gp20
  • Pam3 tube initiator gp17
KeywordsVIRAL PROTEIN / baseplate / VIRUS
Biological speciesuncultured cyanophage (environmental samples)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.19 Å
AuthorsYang, F. / Jiang, Y.L. / Zhou, C.Z.
Funding support China, 1items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2018YFA0903100 China
CitationJournal: Proc Natl Acad Sci U S A / Year: 2023
Title: Fine structure and assembly pattern of a minimal myophage Pam3.
Authors: Feng Yang / Yong-Liang Jiang / Jun-Tao Zhang / Jie Zhu / Kang Du / Rong-Cheng Yu / Zi-Lu Wei / Wen-Wen Kong / Ning Cui / Wei-Fang Li / Yuxing Chen / Qiong Li / Cong-Zhao Zhou /
Abstract: The myophage possesses a contractile tail that penetrates its host cell envelope. Except for investigations on the bacteriophage T4 with a rather complicated structure, the assembly pattern and tail ...The myophage possesses a contractile tail that penetrates its host cell envelope. Except for investigations on the bacteriophage T4 with a rather complicated structure, the assembly pattern and tail contraction mechanism of myophage remain largely unknown. Here, we present the fine structure of a freshwater cyanophage Pam3, which has an icosahedral capsid of ~680 Å in diameter, connected via a three-section neck to an 840-Å-long contractile tail, ending with a three-module baseplate composed of only six protein components. This simplified baseplate consists of a central hub-spike surrounded by six wedge heterotriplexes, to which twelve tail fibers are covalently attached via disulfide bonds in alternating upward and downward configurations. In vitro reduction assays revealed a putative redox-dependent mechanism of baseplate assembly and tail sheath contraction. These findings establish a minimal myophage that might become a user-friendly chassis phage in synthetic biology.
History
DepositionJul 9, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 18, 2023Provider: repository / Type: Initial release
Revision 1.1Feb 1, 2023Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID
Revision 1.2Oct 30, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / em_admin / pdbx_entry_details / pdbx_modification_feature
Item: _em_admin.last_update

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Pam3 baseplate wedge gp22
B: Pam3 baseplate wedge gp22
C: Pam3 baseplate wedge gp23
D: Pam3 baseplate wedge gp23
E: Pam3 baseplate wedge gp22
F: Pam3 baseplate wedge gp22
G: Pam3 baseplate wedge gp23
H: Pam3 baseplate wedge gp22
I: Pam3 baseplate wedge gp22
J: Pam3 baseplate wedge gp23
K: Pam3 baseplate wedge gp22
L: Pam3 baseplate wedge gp22
M: Pam3 baseplate wedge gp23
O: Pam3 baseplate wedge gp22
P: Pam3 baseplate wedge gp22
Q: Pam3 baseplate wedge gp22
R: Pam3 baseplate wedge gp22
S: Pam3 baseplate wedge gp23
X: Pam3 sheath initiator gp21
a: Pam3 tube initiator gp17
b: Pam3 tube initiator gp17
c: Pam3 tube initiator gp17
d: Pam3 tube initiator gp17
e: Pam3 tube initiator gp17
f: Pam3 tube initiator gp17
h: Pam3 plug gp18
i: Pam3 plug gp18
j: Pam3 plug gp18
k: Pam3 plug gp18
l: Pam3 plug gp18
m: Pam3 plug gp18
n: Pam3 sheath initiator gp21
o: Pam3 sheath initiator gp21
p: Pam3 sheath initiator gp21
q: Pam3 sheath initiator gp21
r: Pam3 sheath initiator gp21
t: Pam3 hub gp19
u: Pam3 hub gp19
v: Pam3 hub gp19
w: Pam3 spike gp20
x: Pam3 spike gp20
y: Pam3 spike gp20


Theoretical massNumber of molelcules
Total (without water)968,43842
Polymers968,43842
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

-
Components

-
Pam3 baseplate wedge ... , 2 types, 18 molecules ABEFHIKLOPQRCDGJMS

#1: Protein
Pam3 baseplate wedge gp22


Mass: 32686.787 Da / Num. of mol.: 12 / Source method: isolated from a natural source
Source: (natural) uncultured cyanophage (environmental samples)
#2: Protein
Pam3 baseplate wedge gp23


Mass: 26194.811 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) uncultured cyanophage (environmental samples)

-
Protein , 5 types, 24 molecules Xnopqrabcdefhijklmtuvwxy

#3: Protein
Pam3 sheath initiator gp21


Mass: 13889.669 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) uncultured cyanophage (environmental samples)
#4: Protein
Pam3 tube initiator gp17


Mass: 19854.342 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) uncultured cyanophage (environmental samples)
#5: Protein
Pam3 plug gp18


Mass: 11724.286 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) uncultured cyanophage (environmental samples)
#6: Protein Pam3 hub gp19


Mass: 25201.736 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) uncultured cyanophage (environmental samples)
#7: Protein Pam3 spike gp20


Mass: 23537.537 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) uncultured cyanophage (environmental samples)

-
Details

Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

ComponentName: uncultured cyanophage / Type: VIRUS / Entity ID: all / Source: NATURAL
Source (natural)Organism: uncultured cyanophage (environmental samples)
Details of virusEmpty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRION
Natural hostOrganism: Pseudanabaena mucicola
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 300 K

-
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: SPOT SCAN
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

-
Processing

EM softwareName: RELION / Version: 3.1 / Category: 3D reconstruction
CTF correctionType: PHASE FLIPPING ONLY
3D reconstructionResolution: 3.19 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 45155 / Symmetry type: POINT

+
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