Crystallization and preliminary X-ray diffraction analysis of a high-affinity phosphate-binding protein endowed with phosphatase activity from Pseudomonas aeruginosa PAO1

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Oct;69(Pt 10):1143-6. doi: 10.1107/S1744309113024172. Epub 2013 Sep 28.


In prokaryotes, phosphate starvation induces the expression of numerous phosphate-responsive genes, such as the pst operon including the high-affinity phosphate-binding protein (PBP or pstS) and alkaline phosphatases such as PhoA. This response increases the cellular inorganic phosphate import efficiency. Notably, some Pseudomonas species secrete, via a type-2 secretion system, a phosphate-binding protein dubbed LapA endowed with phosphatase activity. Here, the expression, purification, crystallization and X-ray data collection at 0.87 Å resolution of LapA are described. Combined with biochemical and enzymatic characterization, the structure of this intriguing phosphate-binding protein will help to elucidate the molecular origin of its phosphatase activity and to decipher its putative role in phosphate uptake.

Keywords: LapA; Pseudomonas aeruginosa PAO1; phosphatase; phosphate starvation; phosphate-binding proteins; pstS.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Phosphate-Binding Proteins / chemistry*
  • Phosphoric Monoester Hydrolases / chemistry*
  • Phylogeny
  • Pseudomonas aeruginosa / enzymology*
  • X-Ray Diffraction*


  • Bacterial Proteins
  • Phosphate-Binding Proteins
  • Phosphoric Monoester Hydrolases