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

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

Author Pegos, Vanessa R. Google Scholar
Santos, Rodrigo M. L. Autor UNIFESP Google Scholar
Medrano, Francisco J. Google Scholar
Balan, Andrea Google Scholar
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.
xmlui.dri2xhtml.METS-1.0.item-coverage San Francisco
Language English
Sponsor Coordenagao de Aperfeigoamento de Pessoal de Nivel Superior (CAPES)" for Vanessa Pegos PhD fellowship
Fundagao de Amparo a Pesquisa do Estado de Sao Paulo FAPESP
Grant number CAPES
FAPESP: 2011/20468-1
FAPESP: 2013/09172-9
Date 2017
Published in Plos One. San Francisco, v. 12, n. 5, p. -, 2017.
ISSN 1932-6203 (Sherpa/Romeo, impact factor)
Publisher Public Library Science
Extent -
Origin http://dx.doi.org/10.1371/journal.pone.0178162
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000402058400064
URI https://repositorio.unifesp.br/handle/11600/54453

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