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

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...

Full description

Saved in:
Bibliographic Details
Published in:PloS one 2017-05, Vol.12 (5), p.e0178162-e0178162
Main Authors: Pegos, Vanessa R, Santos, Rodrigo M L, Medrano, Francisco J, Balan, Andrea
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacteria
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Binding proteins
Binding sites
Biology and Life Sciences
Chemotaxis
Cloning
Conformation
Crystal structure
Crystallography, X-Ray
E coli
Escherichia coli
Firmicutes
Gene duplication
Gene Expression Regulation, Bacterial
Genes
Genetic aspects
Ligands
Mycobacterium tuberculosis
Phosphate
Phosphate-Binding Proteins - chemistry
Phosphate-Binding Proteins - genetics
Phosphate-Binding Proteins - metabolism
Phosphates
Phosphates - metabolism
Physical Sciences
Physiological aspects
Phytopathogenic bacteria
Protein Conformation
Proteins
Regulon - genetics
Research and Analysis Methods
Sequence Alignment
Spectrum analysis
Structure
Tuberculosis
Xanthomonas - genetics
Xanthomonas - growth & development
Xanthomonas - metabolism
Xanthomonas citri
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0178162