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In  Escherichia coli , the ATP-Binding Cassette transporter for phosphate is encoded by the  pstSCAB  operon. PstS is the periplasmic component responsible for affinity and specificity of the system and has also been related to a regulatory role and chemotaxis during depletion of phosphate.  Xanthomonas citri  has two phosphate-binding proteins: PstS and PhoX, which are differentially expressed under phosphate limitation. In this work, we focused on PhoX characterization and comparison with PstS. The PhoX three-dimensional structure was solved in a closed conformation with a phosphate engulfed in the binding site pocket between two domains. Comparison between PhoX and PstS revealed that they originated from gene duplication, but despite their similarities they show significant differences in the region that interacts with the permeases.

Structural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citri