3JA7
Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution
Summary for 3JA7
| Entry DOI | 10.2210/pdb3ja7/pdb |
| EMDB information | 6324 |
| Descriptor | Portal protein gp20 (1 entity in total) |
| Functional Keywords | viral protein |
| Biological source | Enterobacteria phage T4 |
| Total number of polymer chains | 12 |
| Total formula weight | 640300.97 |
| Authors | Sun, L.,Zhang, X.,Gao, S.,Rao, P.A.,Padilla-Sanchez, V.,Chen, Z.,Sun, S.,Xiang, Y.,Subramaniam, S.,Rao, V.B.,Rossmann, M.G. (deposition date: 2015-04-21, release date: 2015-07-22, Last modification date: 2024-02-21) |
| Primary citation | Sun, L.,Zhang, X.,Gao, S.,Rao, P.A.,Padilla-Sanchez, V.,Chen, Z.,Sun, S.,Xiang, Y.,Subramaniam, S.,Rao, V.B.,Rossmann, M.G. Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution. Nat Commun, 6:7548-7548, 2015 Cited by PubMed 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. PubMed: 26144253DOI: 10.1038/ncomms8548 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
Download full validation report






