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

Citations Over TimeTop 10% of 2015 papers

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.

Related Papers

• → Characterization of a bacteriophage, isolated from a cow with mastitis, that is lytic against Staphylococcus aureus strains(2011)96 cited
• → Electrophoresis of bacteriophage T7 and T7 capsids in agarose gels(1978)64 cited
• → Recovery and Characterization of Bacteria Resisting Infection by Lytic Bacteriophage(2017)4 cited
• → Isolation and Characterization of an Aeromonas punctata Bacteriophage(2015)1 cited
• → Amino acid sequences from the gene F(Capsid) protein of bacteriophage φX174(1976)18 cited