期刊
STRUCTURE
卷 20, 期 8, 页码 1384-1390出版社
CELL PRESS
DOI: 10.1016/j.str.2012.05.011
关键词
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资金
- NIH [R01 AI040101]
- NCRR [2P41RR017573-11]
- NIGMS [9 P41 GM103310-11]
- FP7 Marie-Curie IOF fellowship [273427]
- National Institutes of Health (National Center for Research Resources) [2P41RR001081]
- National Institutes of Health (National Institute of General Medical Sciences) [9P41GM103311]
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.
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