3J40

Validated Near-Atomic Resolution Structure of Bacteriophage Epsilon15 Derived from Cryo-EM and Modeling


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Validated near-atomic resolution structure of bacteriophage epsilon15 derived from cryo-EM and modeling.

Baker, M.L.Hryc, C.F.Zhang, Q.Wu, W.Jakana, J.Haase-Pettingell, C.Afonine, P.V.Adams, P.D.King, J.A.Jiang, W.Chiu, W.

(2013) Proc Natl Acad Sci U S A 110: 12301-12306

  • DOI: https://doi.org/10.1073/pnas.1309947110
  • Primary Citation of Related Structures:  
    3J40

  • PubMed Abstract: 

    High-resolution structures of viruses have made important contributions to modern structural biology. Bacteriophages, the most diverse and abundant organisms on earth, replicate and infect all bacteria and archaea, making them excellent potential alternatives to antibiotics and therapies for multidrug-resistant bacteria. Here, we improved upon our previous electron cryomicroscopy structure of Salmonella bacteriophage epsilon15, achieving a resolution sufficient to determine the tertiary structures of both gp7 and gp10 protein subunits that form the T = 7 icosahedral lattice. This study utilizes recently established best practice for near-atomic to high-resolution (3-5 Å) electron cryomicroscopy data evaluation. The resolution and reliability of the density map were cross-validated by multiple reconstructions from truly independent data sets, whereas the models of the individual protein subunits were validated adopting the best practices from X-ray crystallography. Some sidechain densities are clearly resolved and show the subunit-subunit interactions within and across the capsomeres that are required to stabilize the virus. The presence of the canonical phage and jellyroll viral protein folds, gp7 and gp10, respectively, in the same virus suggests that epsilon15 may have emerged more recently relative to other bacteriophages.


  • Organizational Affiliation

    National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
gp10111Salmonella phage epsilon15Mutation(s): 0 
UniProt
Find proteins for Q858G5 (Salmonella phage epsilon15)
Explore Q858G5 
Go to UniProtKB:  Q858G5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ858G5
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
gp7335Salmonella phage epsilon15Mutation(s): 0 
UniProt
Find proteins for Q858G8 (Salmonella phage epsilon15)
Explore Q858G8 
Go to UniProtKB:  Q858G8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ858G8
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONEMAN1
RECONSTRUCTIONEMAN2
RECONSTRUCTIONjspr

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-07-10
    Type: Initial release
  • Version 1.1: 2013-07-17
    Changes: Other
  • Version 1.2: 2013-07-24
    Changes: Database references
  • Version 1.3: 2013-08-07
    Changes: Database references
  • Version 1.4: 2018-07-18
    Changes: Data collection
  • Version 1.5: 2024-02-21
    Changes: Data collection, Database references, Derived calculations