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TitleA structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.
Journal, issue, pagesStructure, Vol. 31, Issue 3, Page 282-294.e5, Year 2023
Publish dateMar 2, 2023
AuthorsJennifer M Podgorski / Krista Freeman / Sophia Gosselin / Alexis Huet / James F Conway / Mary Bird / John Grecco / Shreya Patel / Deborah Jacobs-Sera / Graham Hatfull / Johann Peter Gogarten / Janne Ravantti / Simon J White /
PubMed AbstractMany 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. ...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.
External linksStructure / PubMed:36649709 / PubMed Central
MethodsEM (single particle)
Resolution2.2 - 4.0 Å
Structure data

27824

8e16

EMDB-27824, PDB-8e16:
Mycobacterium phage Che8
Method: EM (single particle) / Resolution: 2.5 Å

27992

8eb4

EMDB-27992, PDB-8eb4:
Gordonia phage Ziko
Method: EM (single particle) / Resolution: 2.6 Å

28012

8ec2

EMDB-28012, PDB-8ec2:
Mycobacterium phage Adephagia
Method: EM (single particle) / Resolution: 2.4 Å

28015

8ec8

EMDB-28015, PDB-8ec8:
Mycobacterium phage Bobi
Method: EM (single particle) / Resolution: 2.5 Å

28016

8eci

EMDB-28016, PDB-8eci:
Arthrobacter phage Bridgette
Method: EM (single particle) / Resolution: 4.0 Å

28017

8ecj

EMDB-28017, PDB-8ecj:
Mycobacterium phage Cain
Method: EM (single particle) / Resolution: 2.9 Å

28018

8eck

EMDB-28018, PDB-8eck:
Gordonia phage Cozz
Method: EM (single particle) / Resolution: 2.6 Å

28020

8ecn

EMDB-28020, PDB-8ecn:
Mycobacterium phage Ogopogo
Method: EM (single particle) / Resolution: 2.7 Å

28021

8eco

EMDB-28021, PDB-8eco:
Microbacterium phage Oxtober96
Method: EM (single particle) / Resolution: 2.2 Å

28039

8edu

EMDB-28039, PDB-8edu:
Mycobacteriophage Muddy capsid
Method: EM (single particle) / Resolution: 2.7 Å

Source
  • mycobacterium virus che8
  • gordonia phage ziko (virus)
  • mycobacterium phage adephagia (virus)
  • mycobacterium phage bobi (virus)
  • arthrobacter phage bridgette (virus)
  • mycobacterium phage cain (virus)
  • gordonia phage cozz (virus)
  • mycobacterium phage ogopogo (virus)
  • microbacterium phage oxtober96 (virus)
  • mycobacterium phage muddy (virus)
KeywordsVIRUS / HK97-fold / T=9 / tailed bacteriophage / T=7 / Bacteriophage / Mycobacteriophage / Capsid

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