6Q5U

High resolution electron cryo-microscopy structure of the bacteriophage PR772

Summary for 6Q5U

• Entry DOI: 10.2210/pdb6q5u/pdb
• EMDB information: 4461
• Descriptor: Major Capsid Protein (P3), Minor Capsid Protein (P30), Infectivity Protein (P16), ... (5 entities in total)
• Functional Keywords: phage, tectiviridae, membrane, double-barrel, helix turn helix, helix with a kink, beta-propeller, heteropentamer, penton, virus
• Biological source: Enterobacteria phage PR772; More
• Total number of polymer chains: 19
• Total formula weight: 674924.19

Authors

Narayana Reddy, H.K.,Svenda, M. (deposition date: 2018-12-09, release date: 2019-06-19, Last modification date: 2024-05-15)

Primary citation

Reddy, H.K.,Hajdu, J.,Carroni, M.,Svenda, M.
Electron cryo-microscopy of Bacteriophage PR772 reveals the elusive vertex complex and the capsid architecture.
Elife, 8:-, 2019

PubMed Abstract: Bacteriophage PR772, a member of the 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.

PubMed: 31513011
DOI: 10.7554/eLife.48496

Experimental method

ELECTRON MICROSCOPY (2.75 Å)