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

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

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Aix Marseille Université, URMITE, UM63, CNRS 7278, IRD 198, Inserm 1095, 27 Boulevard Jean Moulin, 13385 Marseille CEDEX 5, France.


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.


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

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