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TitleMaturation in action: CryoEM study of a viral capsid caught during expansion.
Journal, issue, pagesStructure, Vol. 20, Issue 8, Page 1384-1390, Year 2012
Publish dateAug 8, 2012
AuthorsDavid Veesler / Joel Quispe / Nikolaus Grigorieff / Clinton S Potter / Bridget Carragher / John E Johnson /
PubMed AbstractBacteriophage HK97 maturation involves discrete intermediate particle forms, comparable to transitional states in protein folding, before reaching its mature form. The process starts by formation of ...Bacteriophage HK97 maturation involves discrete intermediate particle forms, comparable to transitional states in protein folding, before reaching its mature form. The process starts by formation of a metastable prohead, poised for exothermic expansion triggered by DNA packaging. During maturation, the capsid subunit transitions from a strained to a canonical tertiary conformation and this has been postulated to be the driving mechanism for initiating expansion via switching hexameric capsomer architecture from skewed to 6-fold symmetric. We report the subnanometer electron-cryomicroscopy reconstruction of the HK97 first expansion intermediate before any crosslink formation. This form displays 6-fold symmetric hexamers, but capsid subunit tertiary structures exhibit distortions comparable to the prohead forms. We propose that coat subunit strain release acts in synergy with the first crosslinks to drive forward maturation. Finally, we speculate that the energetic features of this transition may result from increased stability of intermediates during maturation via enhanced inter-subunit interactions.
External linksStructure / PubMed:22748764 / PubMed Central
MethodsEM (single particle)
Resolution9.3 Å
Structure data

EMDB-2112:
Maturation in action: CryoEM study of a viral capsid caught during expansion. (The HK97 first expansion intermediate).
Method: EM (single particle) / Resolution: 9.3 Å

Source
  • Enterobacteria phage HK97 (virus)

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