Crystal structure of a small heat-shock protein from Xylella fastidiosa reveals a distinct high-order structure

Acta Crystallogr F Struct Biol Commun. 2017 Apr 1;73(Pt 4):222-227. doi: 10.1107/S2053230X17004101. Epub 2017 Mar 22.

Abstract

Citrus variegated chlorosis is a disease that attacks economically important citrus plantations and is caused by the plant-pathogenic bacterium Xylella fastidiosa. In this work, the structure of a small heat-shock protein from X. fastidiosa (XfsHSP17.9) is reported. The high-order structures of small heat-shock proteins from other organisms are arranged in the forms of double-disc, hollow-sphere or spherical assemblies. Unexpectedly, the structure reported here reveals a high-order architecture forming a nearly square cavity.

Keywords: XfsHSP17.9; Xylella fastidiosa; chaperones; citrus variegated chlorosis; small heat-shock protein; α-crystallin domain.

MeSH terms

  • Amino Acid Motifs
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Crystallography, X-Ray
  • Heat-Shock Proteins / chemistry*
  • Heat-Shock Proteins / metabolism
  • Heat-Shock Proteins, Small / chemistry*
  • Heat-Shock Proteins, Small / metabolism
  • Models, Molecular
  • Protein Conformation, alpha-Helical
  • Protein Conformation, beta-Strand
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Structural Homology, Protein
  • Xylella / chemistry*
  • Xylella / metabolism

Substances

  • Bacterial Proteins
  • Heat-Shock Proteins
  • Heat-Shock Proteins, Small
  • HspA protein, bacteria
  • Recombinant Proteins