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

Author(s)

Pegos, Vanessa R. ; Santos, Rodrigo M. L. ; Medrano, Francisco J. ; Balan, Andrea

• Document type: Journal article
• Source: PLoS One; v. 12, n. 5 MAY 22 2017.
• Web of Science Citations: 0

Abstract

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. (AU)

• FAPESP's process: 13/09172-9 - Structural and funcional characterization of the sulfate ABC transporter from Xanthomonas axonopodis pv. citri and related enzymes
• Grantee: Andrea Balan Fernandes
• Support Opportunities: Regular Research Grants
• FAPESP's process: 11/20468-1 - Molecular mechanisms involved in pathogen adaptation and virulence, host resistance and symptom development in citrus-bacteria interactions
• Grantee: Celso Eduardo Benedetti
• Support Opportunities: Research Projects - Thematic Grants