6O3H

Icosahedral reconstruction of the thermophilic bacteriophage P74-26 capsid

Summary for 6O3H

• Entry DOI: 10.2210/pdb6o3h/pdb
• EMDB information: 0618
• Descriptor: Major head protein, P74-26 Head Decoration Protein (2 entities in total)
• Functional Keywords: virus, virion, capsid, major capsid protein, decoration protein, icosahedral virus, caudovirus, thermophilic, bacteriophage
• Biological source: Thermus virus P74-26; More
• Total number of polymer chains: 14
• Total formula weight: 441401.69

Authors

Stone, N.P.,Demo, G.,Agnello, E.,Kelch, B.A. (deposition date: 2019-02-26, release date: 2019-07-24, Last modification date: 2024-03-20)

Primary citation

Stone, N.P.,Demo, G.,Agnello, E.,Kelch, B.A.
Principles for enhancing virus capsid capacity and stability from a thermophilic virus capsid structure.
Nat Commun, 10:4471-4471, 2019

PubMed Abstract: The capsids of double-stranded DNA viruses protect the viral genome from the harsh extracellular environment, while maintaining stability against the high internal pressure of packaged DNA. To elucidate how capsids maintain stability in an extreme environment, we use cryoelectron microscopy to determine the capsid structure of thermostable phage P74-26 to 2.8-Å resolution. We find P74-26 capsids exhibit an overall architecture very similar to those of other tailed bacteriophages, allowing us to directly compare structures to derive the structural basis for enhanced stability. Our structure reveals lasso-like interactions that appear to function like catch bonds. This architecture allows the capsid to expand during genome packaging, yet maintain structural stability. The P74-26 capsid has T = 7 geometry despite being twice as large as mesophilic homologs. Capsid capacity is increased with a larger, flatter major capsid protein. Given these results, we predict decreased icosahedral complexity (i.e. T ≤ 7) leads to a more stable capsid assembly.

PubMed: 31578335
DOI: 10.1038/s41467-019-12341-z

Experimental method

ELECTRON MICROSCOPY (2.8 Å)