3H3W

Fitting of the gp6 crystal structure into 3D cryo-EM reconstruction of bacteriophage T4 dome-shaped baseplate

Summary for 3H3W

• Entry DOI: 10.2210/pdb3h3w/pdb
• Related: 3H2T
• EMDB information: 1048
• Descriptor: Baseplate structural protein Gp6 (1 entity in total)
• Functional Keywords: viral structural protein, virion, viral protein
• Biological source: Enterobacteria phage T4 (Bacteriophage T4)
• Total number of polymer chains: 12
• Total formula weight: 459653.39

Authors

Aksyuk, A.A.,Leiman, P.G.,Shneider, M.M.,Mesyanzhinov, V.V.,Rossmann, M.G. (deposition date: 2009-04-17, release date: 2009-05-19, Last modification date: 2024-02-21)

Primary citation

Aksyuk, A.A.,Leiman, P.G.,Shneider, M.M.,Mesyanzhinov, V.V.,Rossmann, M.G.
The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate.
Structure, 17:800-808, 2009

PubMed Abstract: The baseplate of bacteriophage T4 is a multicomponent protein complex, which controls phage attachment to the host. It assembles from six wedges and a central hub. During infection the baseplate undergoes a large conformational change from a dome-shaped to a flat, star-shaped structure. We report the crystal structure of the C-terminal half of gene product (gp) 6 and investigate its motion with respect to the other proteins during the baseplate rearrangement. Six gp6 dimers interdigitate, forming a ring that maintains the integrity of the baseplate in both conformations. One baseplate wedge contains an N-terminal dimer of gp6, whereas neighboring wedges are tied together through the C-terminal dimer of gp6. The dimeric interactions are preserved throughout the rearrangement of the baseplate. However, the hinge angle between the N- and C-terminal parts of gp6 changes by approximately 15 degrees , accounting for a 10 A radial increase in the diameter of the gp6 ring.

PubMed: 19523898
DOI: 10.1016/j.str.2009.04.005

Experimental method

ELECTRON MICROSCOPY (12 Å)