Abstract
Bacteriophage φ{symbol}29 requires scaffolding protein to assemble the 450 × 540 Å prolate prohead with T = 3 symmetry end caps. In infections with a temperature-sensitive mutant scaffolding protein, capsids assemble predominantly into 370 Å diameter isometric particles with T = 3 symmetry that lack a head-tail connector. However, a few larger, 430 Å diameter, particles are also assembled. Cryo-electron microscopy shows that these larger particles are icosahedral with T = 4 symmetry. The prolate prohead, as well as the two isometric capsids with T = 3 and T = 4 symmetry, are composed of similar pentamers and differently skewed hexamers. The skewing of the hexamers in the equatorial region of proheads and in the T = 4 isometric particles reflects their different environments. One of the functions of the scaffolding protein, present in the prohead, may be to stabilize skewed hexamers during assembly.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1723-1727 |
| Number of pages | 5 |
| Journal | Structure |
| Volume | 14 |
| Issue number | 11 |
| DOIs | |
| State | Published - Nov 2006 |
| Externally published | Yes |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
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