Expression, purification and crystallization of the C-terminal LRR domain of Streptococcus pyogenes protein 0843

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May 1;69(Pt 5):559-61. doi: 10.1107/S1744309113009664. Epub 2013 Apr 30.

Abstract

Streptococcus pyogenes protein 0843 (Spy0843) is a recently identified protein with a potential adhesin function. Sequence analysis has shown that Spy0843 contains two leucine-rich repeat (LRR) domains that mediate interactions with the gp340 receptor. Here, the C-terminal LRR domain was overexpressed in Escherichia coli, purified and crystallized in the presence of 1.7-1.8 M ammonium sulfate pH 7.4 as precipitant. Data were collected from a single crystal to 1.59 Å resolution at 100 K at a synchrotron-radiation source. The crystal was found to belong to space group I41, with unit-cell parameters a = b = 121.4, c = 51.5 Å and one molecule in the asymmetric unit. Elucidation of the crystal structure will provide insights into the interactions of Spy0843 with the gp340 receptor and a better understanding of the role of Spy0843 in streptococcal infections.

Keywords: Spy0843; Streptococcus pyogenes; bacterial adhesion; leucine-rich repeats; scavenger receptors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification*
  • Crystallization
  • Gene Expression Regulation, Bacterial*
  • Leucine / chemistry
  • Leucine / metabolism
  • Protein Structure, Tertiary
  • Streptococcal Infections / metabolism
  • Streptococcus pyogenes* / chemistry
  • Streptococcus pyogenes* / genetics

Substances

  • Bacterial Proteins
  • Leucine