TY - JOUR
T1 - Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution
AU - Sun, Lei
AU - Zhang, Xinzheng
AU - Gao, Song
AU - Rao, Prashant A.
AU - Padilla-Sanchez, Victor
AU - Chen, Zhenguo
AU - Sun, Siyang
AU - Xiang, Ye
AU - Subramaniam, Sriram
AU - Rao, Venigalla B.
AU - Rossmann, Michael G.
N1 - Funding Information:
We thank Sheryl Kelly for helping to prepare the manuscript for publication. We are very grateful to Hong Zhou and Xing Zhang, from the University of California, Los Angeles, for making their Titan and K2 Summit detector available for cryo-EM data collection. The authors acknowledge the use of instruments at the Electron Imaging Center for NanoMachines supported by NIH (1S10RR23057 and 1S10OD018111), NSF (DBI-1338135) and CNSI at UCLA. We acknowledge the assistance of Jason Pierson from NIH-FEI Living Lab for cryo-EM data collection and Mario Borgnia from National Cancer Institute, National Institutes of Health (NIH) for cryo-EM data analysis. The work was supported by NIH grant AI 081726 to MGR and VBR and in part by the NSF grant MCB-1411989 to V.B.R. S.G. was partially supported by the National Natural Science Foundation of China (Grant No. 31470275).
PY - 2015/7/6
Y1 - 2015/7/6
N2 - The structure and assembly of bacteriophage T4 has been extensively studied. However, the detailed structure of the portal protein remained unknown. Here we report the structure of the bacteriophage T4 portal assembly, gene product 20 (gp20), determined by cryo-electron microscopy (cryo-EM) to 3.6Å resolution. In addition, analysis of a 10 Å resolution cryo-EM map of an empty prolate T4 head shows how the dodecameric portal assembly interacts with the capsid protein gp23 at the special pentameric vertex. The gp20 structure also verifies that the portal assembly is required for initiating head assembly, for attachment of the packaging motor, and for participation in DNA packaging. Comparison of the Myoviridae T4 portal structure with the known portal structures of φ29, SPP1 and P22, representing Podo-and Siphoviridae, shows that the portal structure probably dates back to a time when self-replicating microorganisms were being established on Earth.
AB - The structure and assembly of bacteriophage T4 has been extensively studied. However, the detailed structure of the portal protein remained unknown. Here we report the structure of the bacteriophage T4 portal assembly, gene product 20 (gp20), determined by cryo-electron microscopy (cryo-EM) to 3.6Å resolution. In addition, analysis of a 10 Å resolution cryo-EM map of an empty prolate T4 head shows how the dodecameric portal assembly interacts with the capsid protein gp23 at the special pentameric vertex. The gp20 structure also verifies that the portal assembly is required for initiating head assembly, for attachment of the packaging motor, and for participation in DNA packaging. Comparison of the Myoviridae T4 portal structure with the known portal structures of φ29, SPP1 and P22, representing Podo-and Siphoviridae, shows that the portal structure probably dates back to a time when self-replicating microorganisms were being established on Earth.
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U2 - 10.1038/ncomms8548
DO - 10.1038/ncomms8548
M3 - Article
C2 - 26144253
AN - SCOPUS:84936116751
VL - 6
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
M1 - 7548
ER -