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@article{1121143,
author = {Němeček, Daniel and Boura, Evžen and Wu, Weimin and Cheng, Naiqian and Plevka, Pavel and Qiao, Jian and Mindich, Leonard and Heymann, J Bernard and Hurley, James H and Steven, Alasdair C},
article_location = {CAMBRIDGE},
article_number = {8},
doi = {http://dx.doi.org/10.1016/j.str.2013.06.007},
keywords = {Bacteriophage phi6; Cystoviridae; cryo-electron microscopy; capsid structure; capsid expansion; segmented genome; conformational change; RNA packaging},
language = {eng},
issn = {0969-2126},
journal = {Structure},
title = {Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid},
url = {http://www.ncbi.nlm.nih.gov/pubmed/23891288},
volume = {21},
year = {2013}
}
TY - JOUR
ID - 1121143
AU - Němeček, Daniel - Boura, Evžen - Wu, Weimin - Cheng, Naiqian - Plevka, Pavel - Qiao, Jian - Mindich, Leonard - Heymann, J Bernard - Hurley, James H - Steven, Alasdair C
PY - 2013
TI - Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid
JF - Structure
VL - 21
IS - 8
SP - 1374-1383
EP - 1374-1383
PB - CELL PRESS
SN - 09692126
KW - Bacteriophage phi6
KW - Cystoviridae
KW - cryo-electron microscopy
KW - capsid structure
KW - capsid expansion
KW - segmented genome
KW - conformational change
KW - RNA packaging
UR - http://www.ncbi.nlm.nih.gov/pubmed/23891288
L2 - http://www.ncbi.nlm.nih.gov/pubmed/23891288
N2 - The cystovirus phi 6 shares several distinct features with other double-stranded RNA (dsRNA) viruses, including the human pathogen, rotavirus: segmented genomes, nonequivalent packing of 120 subunits in its icosahedral capsid, and capsids as compartments for transcription and replication. phi 6 assembles as a dodecahedral procapsid that undergoes major conformational changes as it matures into the spherical capsid. We determined the crystal structure of the capsid protein, P1, revealing a flattened trapezoid subunit with an alpha-helical fold. We also solved the procapsid with cryo-electron microscopy to comparable resolution. Fitting the crystal structure into the procapsid disclosed substantial conformational differences between the two P1 conformers. Maturation via two intermediate states involves remodeling on a similar scale, besides huge rigid-body rotations. The capsid structure and its stepwise maturation that is coupled to sequential packaging of three RNA segments sets the cystoviruses apart from other dsRNA viruses as a dynamic molecular machine.
ER -
NĚMEČEK, Daniel, Evžen BOURA, Weimin WU, Naiqian CHENG, Pavel PLEVKA, Jian QIAO, Leonard MINDICH, J Bernard HEYMANN, James H HURLEY and Alasdair C STEVEN. Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid. \textit{Structure}. CAMBRIDGE: CELL PRESS, 2013, vol.~21, No~8, p.~1374-1383. ISSN~0969-2126. Available from: https://dx.doi.org/10.1016/j.str.2013.06.007.
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