2XD8

Capsid structure of the infectious Prochlorococcus Cyanophage P-SSP7


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.60 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural Changes in a Marine Podovirus Associated with Release of its Genome Into Prochlorococcus

Liu, X.Zhang, Q.Murata, K.Baker, M.L.Sullivan, M.B.Fu, C.Dougherty, M.Schmid, M.F.Osburne, M.S.Chisholm, S.W.Chiu, W.

(2010) Nat Struct Mol Biol 17: 830

  • DOI: https://doi.org/10.1038/nsmb.1823
  • Primary Citation of Related Structures:  
    2XD8

  • PubMed Abstract: 

    Podovirus P-SSP7 infects Prochlorococcus marinus, the most abundant oceanic photosynthetic microorganism. Single-particle cryo-electron microscopy yields icosahedral and asymmetrical structures of infectious P-SSP7 with 4.6-A and 9-A resolution, respectively. The asymmetric reconstruction reveals how symmetry mismatches are accommodated among five of the gene products at the portal vertex. Reconstructions of infectious and empty particles show a conformational change of the 'valve' density in the nozzle, an orientation difference in the tail fibers, a disordering of the C terminus of the portal protein and the disappearance of the core proteins. In addition, cryo-electron tomography of P-SSP7 infecting Prochlorococcus showed the same tail-fiber conformation as that in empty particles. Our observations suggest a mechanism whereby, upon binding to the host cell, the tail fibers induce a cascade of structural alterations of the portal vertex complex that triggers DNA release.


  • Organizational Affiliation

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


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
T7-LIKE CAPSID PROTEIN
A, B, C, D, E
A, B, C, D, E, F, G
375Tiamatvirus PSSP7Mutation(s): 0 
UniProt
Find proteins for Q58N30 (Prochlorococcus phage P-SSP7)
Explore Q58N30 
Go to UniProtKB:  Q58N30
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ58N30
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.60 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONMPSA

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-06-16
    Type: Initial release
  • Version 1.1: 2013-03-20
    Changes: Other, Refinement description, Version format compliance
  • Version 1.2: 2018-10-03
    Changes: Data collection
  • Version 1.3: 2019-10-23
    Changes: Data collection, Other