TY - JOUR
T1 - Determinants of Bacteriophage φ{symbol}29 Head Morphology
AU - Choi, Kyung H.
AU - Morais, Marc C.
AU - Anderson, Dwight L.
AU - Rossmann, Michael G.
N1 - Funding Information:
We thank Cheryl Towell and Sharon Wilder for help in the preparation of this manuscript and Norm Olson for taking the original micrographs of the isometric particles. We thank Jaya S. Koti for helpful discussions. This research was supported by National Science Foundation grant MCB0443899 to M.G.R. and a National Institutes of Health grant DE003606 to D.L.A.
PY - 2006/11
Y1 - 2006/11
N2 - 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.
AB - 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.
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U2 - 10.1016/j.str.2006.09.007
DO - 10.1016/j.str.2006.09.007
M3 - Article
C2 - 17098197
AN - SCOPUS:33846222419
SN - 0969-2126
VL - 14
SP - 1723
EP - 1727
JO - Structure
JF - Structure
IS - 11
ER -