8ECN

Mycobacterium phage Ogopogo

Summary for 8ECN

• Entry DOI: 10.2210/pdb8ecn/pdb
• EMDB information: 28016 28017 28018 28020 28021
• Descriptor: Major capsid protein (1 entity in total)
• Functional Keywords: hk97-fold, t=9, tailed bacteriophage, virus
• Biological source: Mycobacterium phage Ogopogo
• Total number of polymer chains: 9
• Total formula weight: 297297.35

Authors

Podgorski, J.M.,White, S.J. (deposition date: 2022-09-02, release date: 2023-02-01, Last modification date: 2024-06-19)

Primary citation

Podgorski, J.M.,Freeman, K.,Gosselin, S.,Huet, A.,Conway, J.F.,Bird, M.,Grecco, J.,Patel, S.,Jacobs-Sera, D.,Hatfull, G.,Gogarten, J.P.,Ravantti, J.,White, S.J.
A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.
Structure, 31:282-, 2023

PubMed Abstract: Many double-stranded DNA viruses, including tailed bacteriophages (phages) and herpesviruses, use the HK97-fold in their major capsid protein to make the capsomers of the icosahedral viral capsid. After the genome packaging at near-crystalline densities, the capsid is subjected to a major expansion and stabilization step that allows it to withstand environmental stresses and internal high pressure. Several different mechanisms for stabilizing the capsid have been structurally characterized, but how these mechanisms have evolved is still not understood. Using cryo-EM structure determination of 10 capsids, structural comparisons, phylogenetic analyses, and Alphafold predictions, we have constructed a detailed structural dendrogram describing the evolution of capsid structural stability within the actinobacteriophages. We show that the actinobacteriophage major capsid proteins can be classified into 15 groups based upon their HK97-fold.

PubMed: 36649709
DOI: 10.1016/j.str.2022.12.012

Experimental method

ELECTRON MICROSCOPY (2.7 Å)