TY - JOUR
T1 - The structure of Sinorhizobium meliloti phage ΦM12, which has a novel T=19l triangulation number and is the founder of a new group of T4-superfamily phages
AU - Stroupe, M. Elizabeth
AU - Brewer, Tess E.
AU - Sousa, Duncan R.
AU - Jones, Kathryn M.
N1 - Funding Information:
We thank Scott Stagg for useful discussions and Brian Washburn, Christopher Stroupe, and Ann-Marie Torregrossa for reading the manuscript. This work was funded by USDA National Institute of Food and Agriculture, Agriculture and Food Research Initiative award 2010-65108-20582 to K.M.J, and American Heart Association award 10IRG4300065 to M.E.S. Molecular graphics and analyses were performed with the UCSF Chimera package. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco (supported by NIGMS P41-GM103311 ). The EM volumes for both the full and empty shells have been deposited into the EMDB with the codes EMD-5717 and EMD-5718, respectively.
PY - 2014/2
Y1 - 2014/2
N2 - ΦM12 is the first example of a T=19l geometry capsid, encapsulating the recently sequenced genome. Here, we present structures determined by cryo-EM of full and empty capsids. The structure reveals the pattern for assembly of 1140 HK97-like capsid proteins, pointing to interactions at the pseudo 3-fold symmetry axes that hold together the asymmetric unit. The particular smooth surface of the capsid, along with a lack of accessory coat proteins encoded by the genome, suggest that this interface is the primary mechanism for capsid assembly. Two-dimensional averages of the tail, including the neck and baseplate, reveal that ΦM12 has a relatively narrow neck that attaches the tail to the capsid, as well as a three-layer baseplate. When free from DNA, the icosahedral edges expand by about 5. nm, while the vertices stay at the same position, forming a similarly smooth, but bowed, T=19l icosahedral capsid.
AB - ΦM12 is the first example of a T=19l geometry capsid, encapsulating the recently sequenced genome. Here, we present structures determined by cryo-EM of full and empty capsids. The structure reveals the pattern for assembly of 1140 HK97-like capsid proteins, pointing to interactions at the pseudo 3-fold symmetry axes that hold together the asymmetric unit. The particular smooth surface of the capsid, along with a lack of accessory coat proteins encoded by the genome, suggest that this interface is the primary mechanism for capsid assembly. Two-dimensional averages of the tail, including the neck and baseplate, reveal that ΦM12 has a relatively narrow neck that attaches the tail to the capsid, as well as a three-layer baseplate. When free from DNA, the icosahedral edges expand by about 5. nm, while the vertices stay at the same position, forming a similarly smooth, but bowed, T=19l icosahedral capsid.
KW - Bacteriophage
KW - Icosahedral
KW - Myovirus
KW - Sinorhizobium meliloti
KW - T=19
KW - ΦM12
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U2 - 10.1016/j.virol.2013.11.019
DO - 10.1016/j.virol.2013.11.019
M3 - Article
C2 - 24503083
AN - SCOPUS:84891810368
SN - 0042-6822
VL - 450-451
SP - 205
EP - 212
JO - Virology
JF - Virology
ER -