The tail lysozyme complex of bacteriophage T4

Fumio Arisaka, Shuji Kanamaru, Petr Leiman, Michael G. Rossmann

Research output: Contribution to journalReview article

38 Scopus citations

Abstract

The tail baseplate of bacteriophage T4 contains a structurally essential, three-domain protein encoded by gene 5 in which the middle domain possesses lysozyme activity. The gene 5 product (gp5) undergoes post-translational cleavage, allowing the resultant N-terminal domain (gp5*) to assemble into the baseplate as a trimer. The lysozyme activity of the undissociated cleaved gp5 is inhibited until infection has been initiated, when the C-terminal portion of the molecule is detached and the rest of the molecule dissociates into monomers. The 3D structure of the undissociated cleaved gp5, complexed with gp27 (another component of the baseplate), shows that it is a cell-puncturing device that functions to penetrate the outer cell membrane and to locally dissolve the periplasmic cell wall.

Original languageEnglish (US)
Pages (from-to)16-21
Number of pages6
JournalInternational Journal of Biochemistry and Cell Biology
Volume35
Issue number1
DOIs
StatePublished - Jan 1 2003
Externally publishedYes

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Keywords

  • Bacteriophage T4
  • Genes 5 and 27
  • Tail lysozyme complex

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

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