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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Pegos, Vanessa R. ; Santos, Rodrigo M. L. ; Medrano, Francisco J. ; Balan, Andrea
Total Authors: 4
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 type: 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 type: Research Projects - Thematic Grants