Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking

Detalhes bibliográficos
Autor(a) principal: Moura, José J. G.
Data de Publicação: 2005
Outros Autores: Palma, P. Nuno, Lagoutte, Bernard, Krippahl, Ludwig, Guerlesquin, Françoise
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/1659
Resumo: FEBS Letters 579 (2005) 4585–4590
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spelling Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural model obtained by NMR-restrained dockingFerredoxinFerredoxin NADP+-reductaseComplexDocking and NMRFEBS Letters 579 (2005) 4585–4590Abstract Ferredoxin (Fd) and ferredoxin-NADP+-reductase(FNR) are two terminal physiological partners of the photosynthetic electron transport chain. Based on a nuclear magnetic resonance(NMR)-restrained-docking approach, two alternative structural models of the Fd–FNR complex in the presence of NADP+ are proposed. The protein docking simulations were performed with the software BiGGER. NMR titration revealed a 1:1 stoichiometry for the complex and allowed the mapping of the interacting residues at the surface of Fd. The NMR chemical shifts were encoded into distance constraints and used with theoretically calculated electronic coupling between the redox cofactors to propose experimentally validated docked complexes.Elsevier B.V. on behalf of the Federation of European Biochemical SocietiesRUNMoura, José J. G.Palma, P. NunoLagoutte, BernardKrippahl, LudwigGuerlesquin, Françoise2008-09-24T13:51:56Z20052005-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/1659enginfo: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:RCAAP2024-03-11T03:31:38Zoai:run.unl.pt:10362/1659Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:14:47.057522Repositório 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 Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking
title Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking
spellingShingle Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking
Moura, José J. G.
Ferredoxin
Ferredoxin NADP+-reductase
Complex
Docking and NMR
title_short Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking
title_full Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking
title_fullStr Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking
title_full_unstemmed Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking
title_sort Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking
author Moura, José J. G.
author_facet Moura, José J. G.
Palma, P. Nuno
Lagoutte, Bernard
Krippahl, Ludwig
Guerlesquin, Françoise
author_role author
author2 Palma, P. Nuno
Lagoutte, Bernard
Krippahl, Ludwig
Guerlesquin, Françoise
author2_role author
author
author
author
dc.contributor.none.fl_str_mv RUN
dc.contributor.author.fl_str_mv Moura, José J. G.
Palma, P. Nuno
Lagoutte, Bernard
Krippahl, Ludwig
Guerlesquin, Françoise
dc.subject.por.fl_str_mv Ferredoxin
Ferredoxin NADP+-reductase
Complex
Docking and NMR
topic Ferredoxin
Ferredoxin NADP+-reductase
Complex
Docking and NMR
description FEBS Letters 579 (2005) 4585–4590
publishDate 2005
dc.date.none.fl_str_mv 2005
2005-01-01T00:00:00Z
2008-09-24T13:51:56Z
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/10362/1659
url http://hdl.handle.net/10362/1659
dc.language.iso.fl_str_mv eng
language eng
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.publisher.none.fl_str_mv Elsevier B.V. on behalf of the Federation of European Biochemical Societies
publisher.none.fl_str_mv Elsevier B.V. on behalf of the Federation of European Biochemical Societies
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
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