8e16 | pdb_00008e16

Mycobacterium phage Che8

spinqualitylabelsall models 8e16, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8e16 is a 9 chain structure with sequence from Mycobacterium virus Che8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q855K4_9CAUD Publication Abstract from PubMed 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. A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.,Podgorski JM, Freeman K, Gosselin S, Huet A, Conway JF, Bird M, Grecco J, Patel S, Jacobs-Sera D, Hatfull G, Gogarten JP, Ravantti J, White SJ Structure. 2023 Jan 7:S0969-2126(22)00498-1. doi: 10.1016/j.str.2022.12.012. PMID:36649709 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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