Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre

Abstract

Adsorption of T4 bacteriophage to the Escherichia coli host cell is mediated by six long and six short tail fibres. After at least three long tail fibres have bound, short tail fibres extend and bind irreversibly to the core region of the host cell lipopolysaccharide (LPS), serving as inextensible stays during penetration of the cell envelope by the tail tube. The short tail fibres consist of a parallel, in-register, trimer of gene product 12 (gp12). The 1.9 Å crystal structure of a heat and protease-stable fragment of gp12 reveals three new folds: a central right-handed triple β-helix, a globular C-terminal domain containing a β-sandwich and an N-terminal β-structure reminiscent of but different from the adenovirus triple β-spiral. The centre of the C-terminal domain shows weak homology to gp11, a trimeric protein connecting the short fibre to the base-plate, suggesting that the trimerisation motifs of gp11 and gp12 are similar. Repeating sequence motifs suggest that the N-terminal β-structure extends further towards the N terminus and is conserved in the long tail fibre proteins gp34 and gp37.