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 () and Michael G. Rossmann ()
Additional contact information
Lei Sun: Purdue University
Xinzheng Zhang: Purdue University
Song Gao: The Catholic University of America, 620 Michigan Ave. N.E., Washington, DC 20064, USA
Prashant A. Rao: National Cancer Institute, National Institutes of Health
Victor Padilla-Sanchez: The Catholic University of America, 620 Michigan Ave. N.E., Washington, DC 20064, USA
Zhenguo Chen: Purdue University
Siyang Sun: Purdue University
Ye Xiang: Purdue University
Sriram Subramaniam: National Cancer Institute, National Institutes of Health
Venigalla B. Rao: The Catholic University of America, 620 Michigan Ave. N.E., Washington, DC 20064, USA
Michael G. Rossmann: Purdue University

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: 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 Å 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.

Date: 2015
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DOI: 10.1038/ncomms8548

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