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3JA7

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

Summary for 3JA7
Entry DOI10.2210/pdb3ja7/pdb
EMDB information6324
DescriptorPortal protein gp20 (1 entity in total)
Functional Keywordsviral protein
Biological sourceEnterobacteria phage T4
Total number of polymer chains12
Total formula weight640300.97
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 citationSun, 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: 26144253
DOI: 10.1038/ncomms8548
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

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