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 G. Leiman, Jochen Klumpp

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

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 (PG II ) helices arranged as a three-layered “PG II sandwich.” Surface residues on the PG II 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

Keywords

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

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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