3J2O

Model of the bacteriophage T4 fibritin based on the cryo-EM reconstruction of the contracted T4 tail containing the phage collar and whiskers

Summary for 3J2O

• Entry DOI: 10.2210/pdb3j2o/pdb
• Related: 1AA0 1OX3 2BSG 3J2M 3J2N
• EMDB information: 5528
• Descriptor: Fibritin (1 entity in total)
• Functional Keywords: bacteriophage t4, phage neck, collar whiskers, fibritin, gpwac, viral protein
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 6
• Total formula weight: 310667.84

Authors

Fokine, A.,Zhang, Z.,Kanamaru, S.,Bowman, V.D.,Aksyuk, A.A.,Arisaka, F.,Rao, V.B.,Rossmann, M.G. (deposition date: 2012-11-12, release date: 2013-03-06, Last modification date: 2024-02-21)

Primary citation

Fokine, A.,Zhang, Z.,Kanamaru, S.,Bowman, V.D.,Aksyuk, A.A.,Arisaka, F.,Rao, V.B.,Rossmann, M.G.
The molecular architecture of the bacteriophage t4 neck.
J.Mol.Biol., 425:1731-1744, 2013

PubMed Abstract: A hexamer of the bacteriophage T4 tail terminator protein, gp15, attaches to the top of the phage tail stabilizing the contractile sheath and forming the interface for binding of the independently assembled head. Here we report the crystal structure of the gp15 hexamer, describe its interactions in T4 virions that have either an extended tail or a contracted tail, and discuss its structural relationship to other phage proteins. The neck of T4 virions is decorated by the "collar" and "whiskers", made of fibritin molecules. Fibritin acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. The collar and whiskers are environment-sensing devices, regulating the retraction of the long tail fibers under unfavorable conditions, thus preventing infection. Cryo-electron microscopy analysis suggests that twelve fibritin molecules attach to the phage neck with six molecules forming the collar and six molecules forming the whiskers.

PubMed: 23434847
DOI: 10.1016/j.jmb.2013.02.012

Experimental method

ELECTRON MICROSCOPY (25 Å)