4ITV

Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, triple mutant, P212121 form


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.60 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.208 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure and flexibility of nanoscale protein cages designed by symmetric self-assembly.

Lai, Y.T.Tsai, K.L.Sawaya, M.R.Asturias, F.J.Yeates, T.O.

(2013) J Am Chem Soc 135: 7738-7743

  • DOI: https://doi.org/10.1021/ja402277f
  • Primary Citation of Related Structures:  
    4IQ4, 4ITV, 4IVJ

  • PubMed Abstract: 

    Designing protein molecules that self-assemble into complex architectures is an outstanding goal in the area of nanobiotechnology. One design strategy for doing this involves genetically fusing together two natural proteins, each of which is known to form a simple oligomer on its own (e.g., a dimer or trimer). If two such components can be fused in a geometrically predefined configuration, that designed subunit can, in principle, assemble into highly symmetric architectures. Initial experiments showed that a 12-subunit tetrahedral cage, 16 nm in diameter, could be constructed following such a procedure [Padilla, J. E.; et al. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 2217; Lai, Y. T.; et al. Science 2012, 336, 1129]. Here we characterize multiple crystal structures of protein cages constructed in this way, including cages assembled from two mutant forms of the same basic protein subunit. The flexibilities of the designed assemblies and their deviations from the target model are described, along with implications for further design developments.


  • Organizational Affiliation

    Department of Bioengineering, University of California, Los Angeles, California 90095, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Non-haem bromoperoxidase BPO-A2, Matrix protein 1
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J, K, L
456Kitasatospora aureofaciensInfluenza A virus (A/Puerto Rico/8/1934(H1N1))
This entity is chimeric
Mutation(s): 2 
Gene Names: bpoA2BROMOPEROXIDASE A2 and M1 MatrixM
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: 3.60 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.208 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 131.62α = 90
b = 156.61β = 90
c = 321.15γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-07-24
    Type: Initial release
  • Version 1.1: 2017-08-16
    Changes: Refinement description, Source and taxonomy
  • Version 1.2: 2023-09-20
    Changes: Data collection, Database references, Refinement description