The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase

Detalhes bibliográficos
Autor(a) principal: Nobrega, Claudia S.
Data de Publicação: 2016
Outros Autores: Saraiva, Ivo H., Carreira, Cintia, Devreese, Bart, Matzapetakis, Manolis, Pauleta, Sofia R.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/35835
Resumo: We thank Fundacao para a Ciencia e Tecnologia (FCT) for the financial support provided to SRP (PTDC/BIA-PRO/109796/2009), CSN (SFRH/BD/87878/2012) and IHS (SFRH/BPD/84404/2012), and that support the 600 MHz and 800 MHz NMR spectrometers that are part of the National NMR Network (RECI/BBB-BQB/0230/2012).
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spelling The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidaseNeisseriaCopper proteinAzurinLazCytochrome c peroxidaseSolution NMR structureBLUE COPPER PROTEINSPARACOCCUS-PANTOTROPHUS PSEUDOAZURINPSEUDOMONAS-AERUGINOSA AZURINOUTER-MEMBRANE PROTEINALCALIGENES-DENITRIFICANSRESOLUTION STRUCTUREACTIVE-SITESH.8 EPITOPENMR SYSTEMPLASTOCYANINWe thank Fundacao para a Ciencia e Tecnologia (FCT) for the financial support provided to SRP (PTDC/BIA-PRO/109796/2009), CSN (SFRH/BD/87878/2012) and IHS (SFRH/BPD/84404/2012), and that support the 600 MHz and 800 MHz NMR spectrometers that are part of the National NMR Network (RECI/BBB-BQB/0230/2012).Neisseria gonorrhoeae colonizes the genitourinary track, and in these environments, especially in the female host, the bacteria are subjected to low levels of oxygen, and reactive oxygen and nitrosyl species. Here, the biochemical characterization of N. gonorrhoeae Laz is presented, as well as, the solution structure of its soluble domain determined by NMR N. gonorrhoeae Laz is a type 1 copper protein of the azurin-family based on its spectroscopic properties and structure, with a redox potential of 277 +/- 5 mV, at pH 7.0, that behaves as a monomer in solution. The globular Laz soluble domain adopts the Greek-key motif, with the copper center located at one end of the beta-barrel coordinated by Gly48, His49, Cys113, His118 and Met122, in a distorted trigonal geometry. The edge of the His118 imidazole ring is water exposed, in a surface that is proposed to be involved in the interaction with its redox partners. The heterologously expressed Laz was shown to be a competent electron donor to N. gonorrhoeae cytochrome c peroxidase. This is an evidence for its involvement in the mechanism of protection against hydrogen peroxide generated by neighboring lactobacilli in the host environment. (C) 2015 Elsevier B.V. All rights reserved.Molecular, Structural and Cellular Microbiology (MOSTMICRO)Instituto de Tecnologia Química e Biológica António Xavier (ITQB)DQ - Departamento de QuímicaUCIBIO - Applied Molecular Biosciences UnitRUNNobrega, Claudia S.Saraiva, Ivo H.Carreira, CintiaDevreese, BartMatzapetakis, ManolisPauleta, Sofia R.2018-05-02T22:05:11Z2016-022016-02-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article8application/pdfhttp://hdl.handle.net/10362/35835eng0005-2728PURE: 1910384https://doi.org/10.1016/j.bbabio.2015.11.006info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T04:19:31Zoai:run.unl.pt:10362/35835Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:30:22.572045Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase
title The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase
spellingShingle The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase
Nobrega, Claudia S.
Neisseria
Copper protein
Azurin
Laz
Cytochrome c peroxidase
Solution NMR structure
BLUE COPPER PROTEINS
PARACOCCUS-PANTOTROPHUS PSEUDOAZURIN
PSEUDOMONAS-AERUGINOSA AZURIN
OUTER-MEMBRANE PROTEIN
ALCALIGENES-DENITRIFICANS
RESOLUTION STRUCTURE
ACTIVE-SITES
H.8 EPITOPE
NMR SYSTEM
PLASTOCYANIN
title_short The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase
title_full The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase
title_fullStr The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase
title_full_unstemmed The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase
title_sort The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase
author Nobrega, Claudia S.
author_facet Nobrega, Claudia S.
Saraiva, Ivo H.
Carreira, Cintia
Devreese, Bart
Matzapetakis, Manolis
Pauleta, Sofia R.
author_role author
author2 Saraiva, Ivo H.
Carreira, Cintia
Devreese, Bart
Matzapetakis, Manolis
Pauleta, Sofia R.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Molecular, Structural and Cellular Microbiology (MOSTMICRO)
Instituto de Tecnologia Química e Biológica António Xavier (ITQB)
DQ - Departamento de Química
UCIBIO - Applied Molecular Biosciences Unit
RUN
dc.contributor.author.fl_str_mv Nobrega, Claudia S.
Saraiva, Ivo H.
Carreira, Cintia
Devreese, Bart
Matzapetakis, Manolis
Pauleta, Sofia R.
dc.subject.por.fl_str_mv Neisseria
Copper protein
Azurin
Laz
Cytochrome c peroxidase
Solution NMR structure
BLUE COPPER PROTEINS
PARACOCCUS-PANTOTROPHUS PSEUDOAZURIN
PSEUDOMONAS-AERUGINOSA AZURIN
OUTER-MEMBRANE PROTEIN
ALCALIGENES-DENITRIFICANS
RESOLUTION STRUCTURE
ACTIVE-SITES
H.8 EPITOPE
NMR SYSTEM
PLASTOCYANIN
topic Neisseria
Copper protein
Azurin
Laz
Cytochrome c peroxidase
Solution NMR structure
BLUE COPPER PROTEINS
PARACOCCUS-PANTOTROPHUS PSEUDOAZURIN
PSEUDOMONAS-AERUGINOSA AZURIN
OUTER-MEMBRANE PROTEIN
ALCALIGENES-DENITRIFICANS
RESOLUTION STRUCTURE
ACTIVE-SITES
H.8 EPITOPE
NMR SYSTEM
PLASTOCYANIN
description We thank Fundacao para a Ciencia e Tecnologia (FCT) for the financial support provided to SRP (PTDC/BIA-PRO/109796/2009), CSN (SFRH/BD/87878/2012) and IHS (SFRH/BPD/84404/2012), and that support the 600 MHz and 800 MHz NMR spectrometers that are part of the National NMR Network (RECI/BBB-BQB/0230/2012).
publishDate 2016
dc.date.none.fl_str_mv 2016-02
2016-02-01T00:00:00Z
2018-05-02T22:05:11Z
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.uri.fl_str_mv http://hdl.handle.net/10362/35835
url http://hdl.handle.net/10362/35835
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0005-2728
PURE: 1910384
https://doi.org/10.1016/j.bbabio.2015.11.006
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 8
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dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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