Send to

Choose Destination
Nat Commun. 2015 Jul 6;6:7548. doi: 10.1038/ncomms8548.

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

Author information

Department of Biological Sciences, Purdue University, 240S. Martin Jischke Drive, West Lafayette, Indiana 47907-2032, USA.
Department of Biology, The Catholic University of America, 620 Michigan Ave. N.E., Washington, DC 20064, USA.
National Cancer Institute, National Institutes of Health, 50 South Drive, Bldg. 50 Room 4306, Bethesda, Maryland 20892, USA.


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.

[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center