5IM6

Crystal structure of designed two-component self-assembling icosahedral cage I32-28


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 5.59 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.226 
  • R-Value Observed: 0.227 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Accurate design of megadalton-scale two-component icosahedral protein complexes.

Bale, J.B.Gonen, S.Liu, Y.Sheffler, W.Ellis, D.Thomas, C.Cascio, D.Yeates, T.O.Gonen, T.King, N.P.Baker, D.

(2016) Science 353: 389-394

  • DOI: https://doi.org/10.1126/science.aaf8818
  • Primary Citation of Related Structures:  
    5IM4, 5IM5, 5IM6

  • PubMed Abstract: 

    Nature provides many examples of self- and co-assembling protein-based molecular machines, including icosahedral protein cages that serve as scaffolds, enzymes, and compartments for essential biochemical reactions and icosahedral virus capsids, which encapsidate and protect viral genomes and mediate entry into host cells. Inspired by these natural materials, we report the computational design and experimental characterization of co-assembling, two-component, 120-subunit icosahedral protein nanostructures with molecular weights (1.8 to 2.8 megadaltons) and dimensions (24 to 40 nanometers in diameter) comparable to those of small viral capsids. Electron microscopy, small-angle x-ray scattering, and x-ray crystallography show that 10 designs spanning three distinct icosahedral architectures form materials closely matching the design models. In vitro assembly of icosahedral complexes from independently purified components occurs rapidly, at rates comparable to those of viral capsids, and enables controlled packaging of molecular cargo through charge complementarity. The ability to design megadalton-scale materials with atomic-level accuracy and controllable assembly opens the door to a new generation of genetically programmable protein-based molecular machines.


  • Organizational Affiliation

    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA. Graduate Program in Molecular and Cellular Biology, University of Washington, Seattle, WA 98195, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Designed self-assembling icosahedral cage I32-28 trimeric subunit157Burkholderia thailandensis E264Mutation(s): 11 
Gene Names: BTH_I1293DR63_1050
UniProt
Find proteins for Q2SZ09 (Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264))
Explore Q2SZ09 
Go to UniProtKB:  Q2SZ09
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ2SZ09
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Designed self-assembling icosahedral cage I32-28 dimeric subunit165Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539Mutation(s): 10 
Gene Names: DR_2006
UniProt
Find proteins for Q9RSW5 (Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1))
Explore Q9RSW5 
Go to UniProtKB:  Q9RSW5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9RSW5
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 5.59 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.226 
  • R-Value Observed: 0.227 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 284.17α = 90
b = 284.17β = 90
c = 640.47γ = 120
Software Package:
Software NamePurpose
XSCALEdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction
XDSdata reduction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-07-27
    Type: Initial release
  • Version 1.1: 2016-08-10
    Changes: Database references
  • Version 1.2: 2017-11-01
    Changes: Author supporting evidence, Database references, Derived calculations
  • Version 1.3: 2023-09-27
    Changes: Data collection, Database references, Refinement description