Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10362/112081 |
Resumo: | This work was financially supported by Fundacao para a Ciencia e Tecnologia (FCT-MCTES) through project PTDC/BIA-PRO/118377/2010, grants SFRH/BD/85806/2012 (ARC), SFRH/BPD/64917/2009 (MC), DAAD-441.00 and Deutsche Forschungsgemeinschaft Grant Le1171/6-1 (to SL). The access to the EMBL facilities was supported by the EU FP7 infrastructure grants P-Cube (Project Number 227764) and BioStruct-X (Project Number 283570). |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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7160 |
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Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography AnalysisCrystal twinningPeriplasmic aldehyde oxidoreductaseSmall angle X-ray scatteringX-ray crystallographyThis work was financially supported by Fundacao para a Ciencia e Tecnologia (FCT-MCTES) through project PTDC/BIA-PRO/118377/2010, grants SFRH/BD/85806/2012 (ARC), SFRH/BPD/64917/2009 (MC), DAAD-441.00 and Deutsche Forschungsgemeinschaft Grant Le1171/6-1 (to SL). The access to the EMBL facilities was supported by the EU FP7 infrastructure grants P-Cube (Project Number 227764) and BioStruct-X (Project Number 283570).The periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli is a molybdenum enzyme involved in detoxification of aldehydes in the cell. It is an example of an αβγ heterotrimeric enzyme of the xanthine oxidase family of enzymes which does not dimerize via its molybdenum cofactor binding domain. In order to structurally characterize PaoABC, X-ray crystallography and small angle X-ray scattering (SAXS) have been carried out. The protein crystallizes in the presence of 20% (w/v) polyethylene glycol 3350 using the hanging-drop vapour diffusion method. Although crystals were initially twinned, several experiments were done to overcome twinning and lowering the crystallization temperature (293 K to 277 K) was the solution to the problem. The non-twinned crystals used to solve the structure diffract X-rays to beyond 1.80 Å and belong to the C2 space group, with cell parameters a = 109.42 Å, b = 78.08 Å, c = 151.77 Å, β = 99.77°, and one molecule in the asymmetric unit. A molecular replacement solution was found for each subunit separately, using several proteins as search models. SAXS data of PaoABC were also collected showing that, in solution, the protein is also an αβγ heterotrimer.DQ - Departamento de QuímicaCQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)RUNOtrelo-Cardoso, Ana Ritada Silva Correia, Marcia AlexandraSchwuchow, ViolaSvergun, Dmitri I.Romão, Maria JoãoLeimkuehler, SilkeSantos-silva, Teresa Sacadura2021-02-20T23:54:53Z2014-022014-02-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/112081eng1422-0067PURE: 404053https://doi.org/10.3390/ijms15022223info: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:RCAAP2024-05-22T17:50:41Zoai:run.unl.pt:10362/112081Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-22T17:50:41Repositório 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 |
Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis |
title |
Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis |
spellingShingle |
Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis Otrelo-Cardoso, Ana Rita Crystal twinning Periplasmic aldehyde oxidoreductase Small angle X-ray scattering X-ray crystallography |
title_short |
Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis |
title_full |
Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis |
title_fullStr |
Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis |
title_full_unstemmed |
Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis |
title_sort |
Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis |
author |
Otrelo-Cardoso, Ana Rita |
author_facet |
Otrelo-Cardoso, Ana Rita da Silva Correia, Marcia Alexandra Schwuchow, Viola Svergun, Dmitri I. Romão, Maria João Leimkuehler, Silke Santos-silva, Teresa Sacadura |
author_role |
author |
author2 |
da Silva Correia, Marcia Alexandra Schwuchow, Viola Svergun, Dmitri I. Romão, Maria João Leimkuehler, Silke Santos-silva, Teresa Sacadura |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
DQ - Departamento de Química CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE) RUN |
dc.contributor.author.fl_str_mv |
Otrelo-Cardoso, Ana Rita da Silva Correia, Marcia Alexandra Schwuchow, Viola Svergun, Dmitri I. Romão, Maria João Leimkuehler, Silke Santos-silva, Teresa Sacadura |
dc.subject.por.fl_str_mv |
Crystal twinning Periplasmic aldehyde oxidoreductase Small angle X-ray scattering X-ray crystallography |
topic |
Crystal twinning Periplasmic aldehyde oxidoreductase Small angle X-ray scattering X-ray crystallography |
description |
This work was financially supported by Fundacao para a Ciencia e Tecnologia (FCT-MCTES) through project PTDC/BIA-PRO/118377/2010, grants SFRH/BD/85806/2012 (ARC), SFRH/BPD/64917/2009 (MC), DAAD-441.00 and Deutsche Forschungsgemeinschaft Grant Le1171/6-1 (to SL). The access to the EMBL facilities was supported by the EU FP7 infrastructure grants P-Cube (Project Number 227764) and BioStruct-X (Project Number 283570). |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-02 2014-02-01T00:00:00Z 2021-02-20T23:54:53Z |
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/10362/112081 |
url |
http://hdl.handle.net/10362/112081 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1422-0067 PURE: 404053 https://doi.org/10.3390/ijms15022223 |
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 |
mluisa.alvim@gmail.com |
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1817545781895233536 |