Structural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citri
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | https://repositorio.unifesp.br/handle/11600/54453 http://dx.doi.org/10.1371/journal.pone.0178162 |
Resumo: | 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. |
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Pegos, Vanessa R.Santos, Rodrigo M. L. [UNIFESP]Medrano, Francisco J.Balan, Andrea2020-07-13T11:53:12Z2020-07-13T11:53:12Z2017Plos One. San Francisco, v. 12, n. 5, p. -, 2017.1932-6203https://repositorio.unifesp.br/handle/11600/54453http://dx.doi.org/10.1371/journal.pone.0178162WOS000402058400064.pdf10.1371/journal.pone.0178162WOS:000402058400064In 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.Coordenagao de Aperfeigoamento de Pessoal de Nivel Superior (CAPES)" for Vanessa Pegos PhD fellowshipFundagao de Amparo a Pesquisa do Estado de Sao Paulo FAPESPUniv Estadual Campinas, UNICAMP, IB, Campinas, SP, BrazilCtr Nacl Energia & Mat CNPEM, Lab Nacl Biociencias LNBio, Campinas, SP, BrazilUniv Mogi Das Cruzes UMC, Mogi Das Cruzes, SP, BrazilUniv Fed Sao Paulo, UNIFESP, Diadema, SP, BrazilCSIC, Ctr Invest Biol, Madrid, SpainUniv Sao Paulo, Inst Ciencias Biomed II ICBII, Sao Paulo, SP, BrazilUniv Fed Sao Paulo, UNIFESP, Diadema, SP, BrazilCAPESFAPESP: 2011/20468-1FAPESP: 2013/09172-9Web of Science-engPublic Library SciencePlos OneStructural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citriinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleSan Francisco125info:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP11600/544532021-09-28 14:50:56.064metadata only accessoai:repositorio.unifesp.br:11600/54453Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652021-09-28T17:50:56Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Structural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citri |
title |
Structural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citri |
spellingShingle |
Structural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citri Pegos, Vanessa R. |
title_short |
Structural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citri |
title_full |
Structural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citri |
title_fullStr |
Structural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citri |
title_full_unstemmed |
Structural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citri |
title_sort |
Structural features of PhoX, one of the phosphate-binding proteins from Pho regulon of Xanthomonas citri |
author |
Pegos, Vanessa R. |
author_facet |
Pegos, Vanessa R. Santos, Rodrigo M. L. [UNIFESP] Medrano, Francisco J. Balan, Andrea |
author_role |
author |
author2 |
Santos, Rodrigo M. L. [UNIFESP] Medrano, Francisco J. Balan, Andrea |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Pegos, Vanessa R. Santos, Rodrigo M. L. [UNIFESP] Medrano, Francisco J. Balan, Andrea |
description |
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. |
publishDate |
2017 |
dc.date.issued.fl_str_mv |
2017 |
dc.date.accessioned.fl_str_mv |
2020-07-13T11:53:12Z |
dc.date.available.fl_str_mv |
2020-07-13T11:53:12Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Plos One. San Francisco, v. 12, n. 5, p. -, 2017. |
dc.identifier.uri.fl_str_mv |
https://repositorio.unifesp.br/handle/11600/54453 http://dx.doi.org/10.1371/journal.pone.0178162 |
dc.identifier.issn.none.fl_str_mv |
1932-6203 |
dc.identifier.file.none.fl_str_mv |
WOS000402058400064.pdf |
dc.identifier.doi.none.fl_str_mv |
10.1371/journal.pone.0178162 |
dc.identifier.wos.none.fl_str_mv |
WOS:000402058400064 |
identifier_str_mv |
Plos One. San Francisco, v. 12, n. 5, p. -, 2017. 1932-6203 WOS000402058400064.pdf 10.1371/journal.pone.0178162 WOS:000402058400064 |
url |
https://repositorio.unifesp.br/handle/11600/54453 http://dx.doi.org/10.1371/journal.pone.0178162 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.none.fl_str_mv |
Plos One |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
- |
dc.coverage.none.fl_str_mv |
San Francisco |
dc.publisher.none.fl_str_mv |
Public Library Science |
publisher.none.fl_str_mv |
Public Library Science |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
|
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1802764156324020224 |