The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase
Autor(a) principal: | |
---|---|
Data de Publicação: | 2018 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | https://doi.org/10.1038/s41598-018-28453-3 |
Resumo: | Flavodiiron proteins (FDPs) are enzymes with a minimal core of two domains: a metallo-β-lactamase-like, harbouring a diiron center, and a flavodoxin, FMN containing, domains. FDPs are O2 or NO reducing enzymes; for many pathogens, they help mitigate the NO produced by the immune system of the host, and aid survival during fluctuating concentrations concentrations of oxygen. FDPs have a mosaic structure, being predicted to contain multiple extra domains. Clostridium difficile, a threatening human pathogen, encodes two FDPs: one with the two canonical domains, and another with a larger polypeptide chain of 843 amino acids, CD1623, with two extra domains, predicted to be a short-rubredoxin-like and an NAD(P)H:rubredoxin oxidoreductase. This multi-domain protein is the most complex FDP characterized thus far. Each of the predicted domains was characterized and the presence of the predicted cofactors confirmed by biochemical and spectroscopic analysis. Results show that this protein operates as a standalone FDP, receiving electrons directly from NADH, and reducing oxygen to water, precluding the need for extra partners. CD1623 displayed negligible NO reductase activity, and is thus considered an oxygen selective FDP, that may contribute to the survival of C. difficile in the human gut and in the environment. |
id |
RCAP_cd9ade272bf5104d401946f98180a963 |
---|---|
oai_identifier_str |
oai:run.unl.pt:10362/68113 |
network_acronym_str |
RCAP |
network_name_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository_id_str |
7160 |
spelling |
The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductaseGeneralFlavodiiron proteins (FDPs) are enzymes with a minimal core of two domains: a metallo-β-lactamase-like, harbouring a diiron center, and a flavodoxin, FMN containing, domains. FDPs are O2 or NO reducing enzymes; for many pathogens, they help mitigate the NO produced by the immune system of the host, and aid survival during fluctuating concentrations concentrations of oxygen. FDPs have a mosaic structure, being predicted to contain multiple extra domains. Clostridium difficile, a threatening human pathogen, encodes two FDPs: one with the two canonical domains, and another with a larger polypeptide chain of 843 amino acids, CD1623, with two extra domains, predicted to be a short-rubredoxin-like and an NAD(P)H:rubredoxin oxidoreductase. This multi-domain protein is the most complex FDP characterized thus far. Each of the predicted domains was characterized and the presence of the predicted cofactors confirmed by biochemical and spectroscopic analysis. Results show that this protein operates as a standalone FDP, receiving electrons directly from NADH, and reducing oxygen to water, precluding the need for extra partners. CD1623 displayed negligible NO reductase activity, and is thus considered an oxygen selective FDP, that may contribute to the survival of C. difficile in the human gut and in the environment.Instituto de Tecnologia Química e Biológica António Xavier (ITQB)Molecular, Structural and Cellular Microbiology (MOSTMICRO)RUNFolgosa, FilipeMartins, Maria C.Teixeira, Miguel2019-04-29T22:17:04Z2018-12-012018-12-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://doi.org/10.1038/s41598-018-28453-3eng2045-2322PURE: 12417509http://www.scopus.com/inward/record.url?scp=85049686739&partnerID=8YFLogxKhttps://doi.org/10.1038/s41598-018-28453-3info: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:RCAAP2024-03-11T04:32:10Zoai:run.unl.pt:10362/68113Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:34:42.880221Repositório 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 multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase |
title |
The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase |
spellingShingle |
The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase Folgosa, Filipe General |
title_short |
The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase |
title_full |
The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase |
title_fullStr |
The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase |
title_full_unstemmed |
The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase |
title_sort |
The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase |
author |
Folgosa, Filipe |
author_facet |
Folgosa, Filipe Martins, Maria C. Teixeira, Miguel |
author_role |
author |
author2 |
Martins, Maria C. Teixeira, Miguel |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
Instituto de Tecnologia Química e Biológica António Xavier (ITQB) Molecular, Structural and Cellular Microbiology (MOSTMICRO) RUN |
dc.contributor.author.fl_str_mv |
Folgosa, Filipe Martins, Maria C. Teixeira, Miguel |
dc.subject.por.fl_str_mv |
General |
topic |
General |
description |
Flavodiiron proteins (FDPs) are enzymes with a minimal core of two domains: a metallo-β-lactamase-like, harbouring a diiron center, and a flavodoxin, FMN containing, domains. FDPs are O2 or NO reducing enzymes; for many pathogens, they help mitigate the NO produced by the immune system of the host, and aid survival during fluctuating concentrations concentrations of oxygen. FDPs have a mosaic structure, being predicted to contain multiple extra domains. Clostridium difficile, a threatening human pathogen, encodes two FDPs: one with the two canonical domains, and another with a larger polypeptide chain of 843 amino acids, CD1623, with two extra domains, predicted to be a short-rubredoxin-like and an NAD(P)H:rubredoxin oxidoreductase. This multi-domain protein is the most complex FDP characterized thus far. Each of the predicted domains was characterized and the presence of the predicted cofactors confirmed by biochemical and spectroscopic analysis. Results show that this protein operates as a standalone FDP, receiving electrons directly from NADH, and reducing oxygen to water, precluding the need for extra partners. CD1623 displayed negligible NO reductase activity, and is thus considered an oxygen selective FDP, that may contribute to the survival of C. difficile in the human gut and in the environment. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-12-01 2018-12-01T00:00:00Z 2019-04-29T22:17:04Z |
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 |
https://doi.org/10.1038/s41598-018-28453-3 |
url |
https://doi.org/10.1038/s41598-018-28453-3 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
2045-2322 PURE: 12417509 http://www.scopus.com/inward/record.url?scp=85049686739&partnerID=8YFLogxK https://doi.org/10.1038/s41598-018-28453-3 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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 |
repository.mail.fl_str_mv |
|
_version_ |
1799137969242636288 |