Folding and function of repetitive structure in the homotrimeric phage P22 tailspike protein

J Struct Biol. 1998;122(1-2):216-22. doi: 10.1006/jsbi.1998.3974.

Abstract

The Salmonella bacteriophage P22 recognizes its host cell receptor, lipopolysaccharide, by means of six tailspikes, thermostable homotrimers of 72-kDa polypeptides. Biophysical results on the binding reaction, together with high-resolution structural information from X-ray crystallography, have shed light on the interactions determining the viral host range. Folding and assembly of the tailspike protein in vitro have been analyzed in detail, and the data have been compared with observations on the in vivo assembly pathway. Repetitive structural elements in the tailspike protein, like a side-by-side trimer of parallel beta-helices, a parallel alpha-helical bundle, a triangular prism made up from antiparallel beta-sheets, and a short segment of a triple beta-helix can be considered building blocks for larger structural proteins, and thus, the results on P22 tailspike may have implications for fibrous protein structure and folding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteriophage P22 / chemistry*
  • Carbohydrate Sequence
  • Crystallography, X-Ray
  • Glycoside Hydrolases / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding*
  • Protein Structure, Secondary
  • Viral Tail Proteins / chemistry*

Substances

  • Viral Tail Proteins
  • tailspike protein, bacteriophage
  • Glycoside Hydrolases