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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.

Author information

1
Aix Marseille Université, URMITE, UM63, CNRS 7278, IRD 198, Inserm 1095, 27 Boulevard Jean Moulin, 13385 Marseille CEDEX 5, France.

Abstract

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

PMID:
24100568
PMCID:
PMC3792676
DOI:
10.1107/S1744309113024172
[Indexed for MEDLINE]
Free PMC Article

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