EMD-10237

Single-particle
4.41 Å
EMD-10237 Deposition: 19/08/2019
Map released: 25/09/2019
Last modified: 06/11/2019
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-10237

Localized Reconstruction of the vertex region of Bacteriophage PR772 showing the heteropentameric penton

EMD-10237

Single-particle
4.41 Å
EMD-10237 Deposition: 19/08/2019
Map released: 25/09/2019
Last modified: 06/11/2019
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Enterobacteria phage PR772
Sample: Bacteriophage PR772

Deposition Authors: Narayana Reddy HK, Svenda M
Electron cryo-microscopy of Bacteriophage PR772 reveals the elusive vertex complex and the capsid architecture.
Reddy HK , Hajdu J, Carroni M , Svenda M
(2019) eLife , 8
PUBMED: 31513011
DOI: doi:10.7554/eLife.48496
ISSN: 2050-084X
Abstract:
Bacteriophage PR772, a member of the Tectiviridae family, has a 70 nm diameter icosahedral protein capsid that encapsulates a lipid membrane, dsDNA, and various internal proteins. An icosahedrally averaged CryoEM reconstruction of the wild-type virion and a localized reconstruction of the vertex region reveal the composition and the structure of the vertex complex along with new protein conformations that play a vital role in maintaining the capsid architecture of the virion. The overall resolution of the virion is 2.75 Å, while the resolution of the protein capsid is 2.3 Å. The conventional penta-symmetron formed by the capsomeres is replaced by a large vertex complex in the pseudo T = 25 capsid. All the vertices contain the host-recognition protein, P5; two of these vertices show the presence of the receptor-binding protein, P2. The 3D structure of the vertex complex shows interactions with the viral membrane, indicating a possible mechanism for viral infection.