3VDX

Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.281 
  • R-Value Work: 0.229 
  • R-Value Observed: 0.231 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure of a 16-nm cage designed by using protein oligomers.

Lai, Y.T.Cascio, D.Yeates, T.O.

(2012) Science 336: 1129-1129

  • DOI: https://doi.org/10.1126/science.1219351
  • Primary Citation of Related Structures:  
    3VDX, 4D9J

  • PubMed Abstract: 

    Designing protein molecules that will assemble into various kinds of ordered materials represents an important challenge in nanotechnology. We report the crystal structure of a 12-subunit protein cage that self-assembles by design to form a tetrahedral structure roughly 16 nanometers in diameter. The strategy of fusing together oligomeric protein domains can be generalized to produce other kinds of cages or extended materials.


  • Organizational Affiliation

    University of California Los Angeles Biomedical Engineering Interdepartmental Program, Los Angeles, CA 90095, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Designed 16nm tetrahedral protein cage containing Non-haem bromoperoxidase BPO-A2 and Matrix protein 1
A, B, C
456Kitasatospora aureofaciensInfluenza A virus (A/Puerto Rico/8/1934(H1N1))
This entity is chimeric
Mutation(s): 0 
Gene Names: bpoA2BROMOPEROXIDASE A2MM1 Matrix
EC: 1.11.1
UniProt
Find proteins for P29715 (Kitasatospora aureofaciens)
Explore P29715 
Go to UniProtKB:  P29715
Find proteins for P03485 (Influenza A virus (strain A/Puerto Rico/8/1934 H1N1))
Explore P03485 
Go to UniProtKB:  P03485
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsP29715P03485
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.281 
  • R-Value Work: 0.229 
  • R-Value Observed: 0.231 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 122.59α = 90
b = 127.71β = 90
c = 204.22γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction
HKL-3000data collection
XDSdata reduction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-06-20
    Type: Initial release
  • Version 1.1: 2017-08-02
    Changes: Refinement description, Source and taxonomy
  • Version 1.2: 2023-09-13
    Changes: Data collection, Database references, Refinement description