Crystallization and preliminary X‐ray diffraction analysis of a high‐affinity phosphate‐binding protein endowed with phosphatase activity from Pseudomonas aeruginosa PAO1. Issue 10 (8th October 2013)

• Record Type: Journal Article
• Authors: Djeghader, Ahmed; Gotthard, Guillaume; Suh, Andrew; Gonzalez, Daniel; Scott, Ken; Chabriere, Eric; Elias, Mikael
• Is Part Of: Acta crystallographica. Volume 69:Issue 10(2013:Oct.)
• Page Start: 1143
• Page End: 1146
• Publication Date: 2013-10-08
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113024172
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>In prokaryotes, phosphate starvation induces the expression of numerous phosphate‐responsive genes, such as the <italic>pst</italic> 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 <italic>Pseudomonas</italic> species secrete, <italic>via</italic> 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.</p> </abstract>