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Structure. 2018 Dec 4;26(12):1565-1567. doi: 10.1016/j.str.2018.11.008.

A Tail of Phage Adhesins.

Author information

1
Department of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107, USA.
2
Department of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107, USA. Electronic address: gino.cingolani@jefferson.edu.

Abstract

In this issue of Structure, Dunne et al. (2018) unveil the architecture of Salmonella phage S16 adhesin. The structure unravels a beads-on-a-string topology consisting of three domains of which the C-terminal glycine-rich PGII domain, located at the distal tip of the long tail fiber, mediates cell surface attachment and host recognition.

PMID:
30517883
DOI:
10.1016/j.str.2018.11.008

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