Salmonella Phage S16 Tail Fiber Adhesin Features a Rare Polyglycine Rich Domain for Host Recognition

Matthew Dunne, Jenna M. Denyes, Helena Arndt, Martin J. Loessner, Petr Leiman, Jochen Klumpp

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Dunne et al. present the crystal structure of the adhesin tip (gp38) of the Salmonella bacteriophage S16 long tail fiber. Gp38 contains rare polyglycine type II (PGII) helices arranged as a three-layered “PGII sandwich.” Surface residues on the PGII sandwich are key determinants of phage-host interaction.

Original languageEnglish (US)
Pages (from-to)1573-1582.e4
JournalStructure
Volume26
Issue number12
DOIs
StatePublished - Dec 4 2018

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Salmonella Phages
Bacteriophages
polyglycine

Keywords

  • bacteriophage
  • polyglycine sandwich
  • polyglycine type II helix
  • Salmonella
  • X-ray crystallography

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Salmonella Phage S16 Tail Fiber Adhesin Features a Rare Polyglycine Rich Domain for Host Recognition. / Dunne, Matthew; Denyes, Jenna M.; Arndt, Helena; Loessner, Martin J.; Leiman, Petr; Klumpp, Jochen.

In: Structure, Vol. 26, No. 12, 04.12.2018, p. 1573-1582.e4.

Research output: Contribution to journalArticle

Dunne, Matthew ; Denyes, Jenna M. ; Arndt, Helena ; Loessner, Martin J. ; Leiman, Petr ; Klumpp, Jochen. / Salmonella Phage S16 Tail Fiber Adhesin Features a Rare Polyglycine Rich Domain for Host Recognition. In: Structure. 2018 ; Vol. 26, No. 12. pp. 1573-1582.e4.
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