The Structure of Gene Product 6 of Bacteriophage T4, the Hinge-Pin of the Baseplate

Anastasia A. Aksyuk, Petr Leiman, Mikhail M. Shneider, Vadim V. Mesyanzhinov, Michael G. Rossmann

Research output: Contribution to journalArticle

23 Scopus citations

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 ∼15°, accounting for a 10 Å radial increase in the diameter of the gp6 ring.

Original languageEnglish (US)
Pages (from-to)800-808
Number of pages9
JournalStructure
Volume17
Issue number6
DOIs
StatePublished - Jun 10 2009
Externally publishedYes

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Keywords

  • PROTEINS

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Aksyuk, A. A., Leiman, P., Shneider, M. M., Mesyanzhinov, V. V., & Rossmann, M. G. (2009). The Structure of Gene Product 6 of Bacteriophage T4, the Hinge-Pin of the Baseplate. Structure, 17(6), 800-808. https://doi.org/10.1016/j.str.2009.04.005