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

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dc.citation.issue5
dc.citation.volume12
dc.contributor.authorPegos, Vanessa R.
dc.contributor.authorSantos, Rodrigo M. L. [UNIFESP]
dc.contributor.authorMedrano, Francisco J.
dc.contributor.authorBalan, Andrea
dc.coverageSan Francisco
dc.date.accessioned2020-07-13T11:53:12Z
dc.date.available2020-07-13T11:53:12Z
dc.date.issued2017
dc.description.abstractIn 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.en
dc.description.affiliationUniv Estadual Campinas, UNICAMP, IB, Campinas, SP, Brazil
dc.description.affiliationCtr Nacl Energia & Mat CNPEM, Lab Nacl Biociencias LNBio, Campinas, SP, Brazil
dc.description.affiliationUniv Mogi Das Cruzes UMC, Mogi Das Cruzes, SP, Brazil
dc.description.affiliationUniv Fed Sao Paulo, UNIFESP, Diadema, SP, Brazil
dc.description.affiliationCSIC, Ctr Invest Biol, Madrid, Spain
dc.description.affiliationUniv Sao Paulo, Inst Ciencias Biomed II ICBII, Sao Paulo, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, UNIFESP, Diadema, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipCoordenagao de Aperfeigoamento de Pessoal de Nivel Superior (CAPES)" for Vanessa Pegos PhD fellowship
dc.description.sponsorshipFundagao de Amparo a Pesquisa do Estado de Sao Paulo FAPESP
dc.description.sponsorshipIDCAPES
dc.description.sponsorshipIDFAPESP: 2011/20468-1
dc.description.sponsorshipIDFAPESP: 2013/09172-9
dc.format.extent-
dc.identifierhttp://dx.doi.org/10.1371/journal.pone.0178162
dc.identifier.citationPlos One. San Francisco, v. 12, n. 5, p. -, 2017.
dc.identifier.doi10.1371/journal.pone.0178162
dc.identifier.fileWOS000402058400064.pdf
dc.identifier.issn1932-6203
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/54453
dc.identifier.wosWOS:000402058400064
dc.language.isoeng
dc.publisherPublic Library Science
dc.relation.ispartofPlos One
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleStructural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citrien
dc.typeinfo:eu-repo/semantics/article
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