Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution

Lei Sun; Xinzheng Zhang; Song Gao; Prashant A. Rao; Victor Padilla-Sanchez; Zhenguo Chen; Siyang Sun; Ye Xiang; Sriram Subramaniam; Venigalla B. Rao; Michael G. Rossmann

doi:10.1038/ncomms8548

Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution

Lei Sun, Xinzheng Zhang, Song Gao, Prashant A. Rao, Victor Padilla-Sanchez, Zhenguo Chen, Siyang Sun, Ye Xiang, Sriram Subramaniam, Venigalla B. Rao, Michael G. Rossmann

Research output: Contribution to journal › Article

44 Scopus citations

Abstract

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.

Original language	English (US)
Article number	7548
Journal	Nature Communications
Volume	6
DOIs	https://doi.org/10.1038/ncomms8548
Publication status	Published - Jul 6 2015

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ASJC Scopus subject areas

Chemistry(all)
Biochemistry, Genetics and Molecular Biology(all)
Physics and Astronomy(all)

Cite this

Sun, L., Zhang, X., Gao, S., Rao, P. A., Padilla-Sanchez, V., Chen, Z., ... Rossmann, M. G. (2015). Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution. Nature Communications, 6, [7548]. https://doi.org/10.1038/ncomms8548

Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution. / Sun, Lei; Zhang, Xinzheng; Gao, Song; Rao, Prashant A.; Padilla-Sanchez, Victor; Chen, Zhenguo; Sun, Siyang; Xiang, Ye; Subramaniam, Sriram; Rao, Venigalla B.; Rossmann, Michael G.

In: Nature Communications, Vol. 6, 7548, 06.07.2015.

Research output: Contribution to journal › Article

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abstract = "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 3.6{\AA} resolution. In addition, analysis of a 10 {\AA} 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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10.1038/ncomms8548