[English] 日本語
Yorodumi
- EMDB-47039: Pseudosymmetric protein nanocage GI16-F7 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-47039
TitlePseudosymmetric protein nanocage GI16-F7
Map data
Sample
  • Complex: Pseudosymmetric protein nanocages: GI9-F7 nanocage
    • Protein or peptide: Pseudosymmetric protein nanocage GI16-F7 A Chain
    • Protein or peptide: Pseudosymmetric protein nanocage GI16-F7 B Chain
    • Protein or peptide: Pseudosymmetric protein nanocage GI16-F7 C Chain
KeywordsFusion protein / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / pseudosymmetric protein nanocages / VIRAL PROTEIN
Biological speciessynthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 14.9 Å
AuthorsPark YJ / Dowling QM / Seattle Structural Genomics Center for Infectious Disease (SSGCID) / King NP / Veesler D
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI158186 United States
CitationJournal: Nature / Year: 2025
Title: Hierarchical design of pseudosymmetric protein nanocages.
Authors: Quinton M Dowling / Young-Jun Park / Chelsea N Fries / Neil C Gerstenmaier / Sebastian Ols / Erin C Yang / Adam J Wargacki / Annie Dosey / Yang Hsia / Rashmi Ravichandran / Carl D Walkey / ...Authors: Quinton M Dowling / Young-Jun Park / Chelsea N Fries / Neil C Gerstenmaier / Sebastian Ols / Erin C Yang / Adam J Wargacki / Annie Dosey / Yang Hsia / Rashmi Ravichandran / Carl D Walkey / Anika L Burrell / David Veesler / David Baker / Neil P King /
Abstract: Discrete protein assemblies ranging from hundreds of kilodaltons to hundreds of megadaltons in size are a ubiquitous feature of biological systems and perform highly specialized functions. Despite ...Discrete protein assemblies ranging from hundreds of kilodaltons to hundreds of megadaltons in size are a ubiquitous feature of biological systems and perform highly specialized functions. Despite remarkable recent progress in accurately designing new self-assembling proteins, the size and complexity of these assemblies has been limited by a reliance on strict symmetry. Here, inspired by the pseudosymmetry observed in bacterial microcompartments and viral capsids, we developed a hierarchical computational method for designing large pseudosymmetric self-assembling protein nanomaterials. We computationally designed pseudosymmetric heterooligomeric components and used them to create discrete, cage-like protein assemblies with icosahedral symmetry containing 240, 540 and 960 subunits. At 49, 71 and 96 nm diameter, these nanocages are the largest bounded computationally designed protein assemblies generated to date. More broadly, by moving beyond strict symmetry, our work substantially broadens the variety of self-assembling protein architectures that are accessible through design.
History
DepositionSep 17, 2024-
Header (metadata) releaseJan 1, 2025-
Map releaseJan 1, 2025-
UpdateFeb 26, 2025-
Current statusFeb 26, 2025Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_47039.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
2.84 Å/pix.
x 600 pix.
= 1704. Å
2.84 Å/pix.
x 600 pix.
= 1704. Å
2.84 Å/pix.
x 600 pix.
= 1704. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 2.84 Å
Density
Contour LevelBy AUTHOR: 1.3
Minimum - Maximum-0.21439731 - 1.7495959
Average (Standard dev.)0.006968156 (±0.122478835)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions600600600
Spacing600600600
CellA=B=C: 1704.0 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Additional map: #1

Fileemd_47039_additional_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #1

Fileemd_47039_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: #2

Fileemd_47039_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Pseudosymmetric protein nanocages: GI9-F7 nanocage

EntireName: Pseudosymmetric protein nanocages: GI9-F7 nanocage
Components
  • Complex: Pseudosymmetric protein nanocages: GI9-F7 nanocage
    • Protein or peptide: Pseudosymmetric protein nanocage GI16-F7 A Chain
    • Protein or peptide: Pseudosymmetric protein nanocage GI16-F7 B Chain
    • Protein or peptide: Pseudosymmetric protein nanocage GI16-F7 C Chain

-
Supramolecule #1: Pseudosymmetric protein nanocages: GI9-F7 nanocage

SupramoleculeName: Pseudosymmetric protein nanocages: GI9-F7 nanocage / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: synthetic construct (others)

-
Macromolecule #1: Pseudosymmetric protein nanocage GI16-F7 A Chain

MacromoleculeName: Pseudosymmetric protein nanocage GI16-F7 A Chain / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: synthetic construct (others)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GSHHHHHHGS EKAAKAEEAA RKMEELFKEH KIVAVLRANS VEEAKKKALA VFLGGVHLIE ITFTVPDADT VIKELSFLKE MGAIIGAGTV TSVEQCREAV ESGAEFIVSP HLDEEISQFC KEEGVFYMPG VMTPTELYKA MKLGHTILKL FPGEVVGPQF VEAMKGPFPN ...String:
GSHHHHHHGS EKAAKAEEAA RKMEELFKEH KIVAVLRANS VEEAKKKALA VFLGGVHLIE ITFTVPDADT VIKELSFLKE MGAIIGAGTV TSVEQCREAV ESGAEFIVSP HLDEEISQFC KEEGVFYMPG VMTPTELYKA MKLGHTILKL FPGEVVGPQF VEAMKGPFPN VKFVPTGGVN LDNVCEWFEA GVLAVGVGSA LVEGTPVEVA EKAKAFVEKI EGCTE

-
Macromolecule #2: Pseudosymmetric protein nanocage GI16-F7 B Chain

MacromoleculeName: Pseudosymmetric protein nanocage GI16-F7 B Chain / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: synthetic construct (others)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MKMEELFKEH KIVAVLRANS VEEAISKALA VFAGGVHLIE ITFTVPDADQ VIKELEFLKE AGAIIGAGTV TSVEQCREAV ESGAEFIVSF HLDEEISQFC KEEGVFYMPG VMTPTELVKA MKLGHTILKL VPGEVVGPQF VEAMKGPFPN VKFVPTGGVN LDNVCEWFEA ...String:
MKMEELFKEH KIVAVLRANS VEEAISKALA VFAGGVHLIE ITFTVPDADQ VIKELEFLKE AGAIIGAGTV TSVEQCREAV ESGAEFIVSF HLDEEISQFC KEEGVFYMPG VMTPTELVKA MKLGHTILKL VPGEVVGPQF VEAMKGPFPN VKFVPTGGVN LDNVCEWFEA GVLAVGVGSA LVEGEPAEVA ELAIRFVEKI RGCTE

-
Macromolecule #3: Pseudosymmetric protein nanocage GI16-F7 C Chain

MacromoleculeName: Pseudosymmetric protein nanocage GI16-F7 C Chain / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: synthetic construct (others)
SequenceString: MKMEELFKEH KIVAVLRANS REEAIEIALA VFAGGVHLIE ITFTVPDADE VIKRLEMLKR AGAIIGAGTV TSVEQCREAV ESGAEFIVSP HLDEEISQFC KEEGVFYMPG VMTPTELVKA MKLGHTILKL FPGEVVGPQF VEAMKGPFPN VKFVPTGGVN LDNVCEWFEA ...String:
MKMEELFKEH KIVAVLRANS REEAIEIALA VFAGGVHLIE ITFTVPDADE VIKRLEMLKR AGAIIGAGTV TSVEQCREAV ESGAEFIVSP HLDEEISQFC KEEGVFYMPG VMTPTELVKA MKLGHTILKL FPGEVVGPQF VEAMKGPFPN VKFVPTGGVN LDNVCEWFEA GVLAVGVGSA LVEGKPSEVA EKARRFVKKI RGCTEGSLEH HHHHH

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 14.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 1083
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING

+
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