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

Ahmed Djeghader, Guillaume Gotthard, Andrew Suh, Daniel Gonzalez, Ken Scott, Eric Chabriere, Mikael Elias

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1143-1146
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number10
DOIs
StatePublished - Oct 2013

Keywords

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

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