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Mycobacterium phage Che8


ABSTRACT:

SUBMITTER: Simon James White 

PROVIDER: EMPIAR-11190 | biostudies-other |

REPOSITORIES: biostudies-other

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Publications

A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.

Podgorski Jennifer M JM   Freeman Krista K   Gosselin Sophia S   Huet Alexis A   Conway James F JF   Bird Mary M   Grecco John J   Patel Shreya S   Jacobs-Sera Deborah D   Hatfull Graham G   Gogarten Johann Peter JP   Ravantti Janne J   White Simon J SJ  

Structure (London, England : 1993) 20230116 3


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  ...[more]

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