Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?

Autores
Klinke, Sebastian; Zylberman, Vanesa; Vega, Daniel Roberto; Guimarães, Beatriz G.; Braden, Bradford C.; Goldbaum, Fernando Alberto
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The enzyme lumazine synthase (LS) catalyzes the penultimate step of riboflavin biosynthesis in plants, fungi and bacteria. The quaternary structure of the polypeptide differs between species, existing as pentamers or as icosahedrally arranged dodecamers of pentamers with 60 subunits. The pathogen Brucella spp. expresses two proteins that exhibit LS activity, RibH1 and RibH2. The latter enzyme belongs to a novel third category of quaternary arrangement for LS, that of a decameric structure assembled as a head-to-head oriented dimer of pentamers. In contrast, the RibH1 enzyme is assembled as a pentamer, as noted for several other LS enzymes. RibH1 appears to be the functional LS in Brucella spp., whereas RibH2, an enzyme of lower catalytic activity, is a virulence factor presumably acting in response to oxidative stress. The latter observation prompted us to further investigate the structural and catalytic properties of RibH2 in order to clarify the biological function of this enzyme. Here, we present a detailed analysis of two new crystallographic forms of RibH2 that explain the low catalytic activity of this enzyme in comparison with RibH1 and other LSs. Additionally, we analyze the effect of pH on the structure of this enzyme, and the binding of riboflavin and 6,7-dimethyl-8-ribityllumazine to its active site.
Fil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Zylberman, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Vega, Daniel Roberto. Comisión Nacional de Energía Atómica; Argentina
Fil: Guimarães, Beatriz G.. Laboratorio Nacional de Luz Sincrotron; Brasil
Fil: Braden, Bradford C.. Bowie State University; Estados Unidos
Fil: Goldbaum, Fernando Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Materia
6,7-Dimethyl-8-Ribityllumazine Synthase
Brucella Spp.
Quaternary Arrangement
Riboflavin Biosynthesis
X-Ray Crystallography
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/39121
Acceder
id CONICETDig_9a6e69d4212eb741070bc4f72abcce3a
oai_identifier_str oai:ri.conicet.gov.ar:11336/39121
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?Klinke, SebastianZylberman, VanesaVega, Daniel RobertoGuimarães, Beatriz G.Braden, Bradford C.Goldbaum, Fernando Alberto6,7-Dimethyl-8-Ribityllumazine SynthaseBrucella Spp.Quaternary ArrangementRiboflavin BiosynthesisX-Ray Crystallographyhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3The enzyme lumazine synthase (LS) catalyzes the penultimate step of riboflavin biosynthesis in plants, fungi and bacteria. The quaternary structure of the polypeptide differs between species, existing as pentamers or as icosahedrally arranged dodecamers of pentamers with 60 subunits. The pathogen Brucella spp. expresses two proteins that exhibit LS activity, RibH1 and RibH2. The latter enzyme belongs to a novel third category of quaternary arrangement for LS, that of a decameric structure assembled as a head-to-head oriented dimer of pentamers. In contrast, the RibH1 enzyme is assembled as a pentamer, as noted for several other LS enzymes. RibH1 appears to be the functional LS in Brucella spp., whereas RibH2, an enzyme of lower catalytic activity, is a virulence factor presumably acting in response to oxidative stress. The latter observation prompted us to further investigate the structural and catalytic properties of RibH2 in order to clarify the biological function of this enzyme. Here, we present a detailed analysis of two new crystallographic forms of RibH2 that explain the low catalytic activity of this enzyme in comparison with RibH1 and other LSs. Additionally, we analyze the effect of pH on the structure of this enzyme, and the binding of riboflavin and 6,7-dimethyl-8-ribityllumazine to its active site.Fil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Zylberman, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Vega, Daniel Roberto. Comisión Nacional de Energía Atómica; ArgentinaFil: Guimarães, Beatriz G.. Laboratorio Nacional de Luz Sincrotron; BrasilFil: Braden, Bradford C.. Bowie State University; Estados UnidosFil: Goldbaum, Fernando Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaElsevier2005-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/39121Klinke, Sebastian; Zylberman, Vanesa; Vega, Daniel Roberto; Guimarães, Beatriz G.; Braden, Bradford C.; et al.; Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?; Elsevier; Journal Of Molecular Biology; 353; 1; 10-2005; 124-1370022-28361089-8638CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S002228360500954Xinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmb.2005.08.017info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:54:38Zoai:ri.conicet.gov.ar:11336/39121instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:54:38.729CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?
title Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?
spellingShingle Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?
Klinke, Sebastian
6,7-Dimethyl-8-Ribityllumazine Synthase
Brucella Spp.
Quaternary Arrangement
Riboflavin Biosynthesis
X-Ray Crystallography
title_short Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?
title_full Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?
title_fullStr Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?
title_full_unstemmed Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?
title_sort Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?
dc.creator.none.fl_str_mv Klinke, Sebastian
Zylberman, Vanesa
Vega, Daniel Roberto
Guimarães, Beatriz G.
Braden, Bradford C.
Goldbaum, Fernando Alberto
author Klinke, Sebastian
author_facet Klinke, Sebastian
Zylberman, Vanesa
Vega, Daniel Roberto
Guimarães, Beatriz G.
Braden, Bradford C.
Goldbaum, Fernando Alberto
author_role author
author2 Zylberman, Vanesa
Vega, Daniel Roberto
Guimarães, Beatriz G.
Braden, Bradford C.
Goldbaum, Fernando Alberto
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv 6,7-Dimethyl-8-Ribityllumazine Synthase
Brucella Spp.
Quaternary Arrangement
Riboflavin Biosynthesis
X-Ray Crystallography
topic 6,7-Dimethyl-8-Ribityllumazine Synthase
Brucella Spp.
Quaternary Arrangement
Riboflavin Biosynthesis
X-Ray Crystallography
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv The enzyme lumazine synthase (LS) catalyzes the penultimate step of riboflavin biosynthesis in plants, fungi and bacteria. The quaternary structure of the polypeptide differs between species, existing as pentamers or as icosahedrally arranged dodecamers of pentamers with 60 subunits. The pathogen Brucella spp. expresses two proteins that exhibit LS activity, RibH1 and RibH2. The latter enzyme belongs to a novel third category of quaternary arrangement for LS, that of a decameric structure assembled as a head-to-head oriented dimer of pentamers. In contrast, the RibH1 enzyme is assembled as a pentamer, as noted for several other LS enzymes. RibH1 appears to be the functional LS in Brucella spp., whereas RibH2, an enzyme of lower catalytic activity, is a virulence factor presumably acting in response to oxidative stress. The latter observation prompted us to further investigate the structural and catalytic properties of RibH2 in order to clarify the biological function of this enzyme. Here, we present a detailed analysis of two new crystallographic forms of RibH2 that explain the low catalytic activity of this enzyme in comparison with RibH1 and other LSs. Additionally, we analyze the effect of pH on the structure of this enzyme, and the binding of riboflavin and 6,7-dimethyl-8-ribityllumazine to its active site.
Fil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Zylberman, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Vega, Daniel Roberto. Comisión Nacional de Energía Atómica; Argentina
Fil: Guimarães, Beatriz G.. Laboratorio Nacional de Luz Sincrotron; Brasil
Fil: Braden, Bradford C.. Bowie State University; Estados Unidos
Fil: Goldbaum, Fernando Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
description The enzyme lumazine synthase (LS) catalyzes the penultimate step of riboflavin biosynthesis in plants, fungi and bacteria. The quaternary structure of the polypeptide differs between species, existing as pentamers or as icosahedrally arranged dodecamers of pentamers with 60 subunits. The pathogen Brucella spp. expresses two proteins that exhibit LS activity, RibH1 and RibH2. The latter enzyme belongs to a novel third category of quaternary arrangement for LS, that of a decameric structure assembled as a head-to-head oriented dimer of pentamers. In contrast, the RibH1 enzyme is assembled as a pentamer, as noted for several other LS enzymes. RibH1 appears to be the functional LS in Brucella spp., whereas RibH2, an enzyme of lower catalytic activity, is a virulence factor presumably acting in response to oxidative stress. The latter observation prompted us to further investigate the structural and catalytic properties of RibH2 in order to clarify the biological function of this enzyme. Here, we present a detailed analysis of two new crystallographic forms of RibH2 that explain the low catalytic activity of this enzyme in comparison with RibH1 and other LSs. Additionally, we analyze the effect of pH on the structure of this enzyme, and the binding of riboflavin and 6,7-dimethyl-8-ribityllumazine to its active site.
publishDate 2005
dc.date.none.fl_str_mv 2005-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/39121
Klinke, Sebastian; Zylberman, Vanesa; Vega, Daniel Roberto; Guimarães, Beatriz G.; Braden, Bradford C.; et al.; Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?; Elsevier; Journal Of Molecular Biology; 353; 1; 10-2005; 124-137
0022-2836
1089-8638
CONICET Digital
CONICET
url http://hdl.handle.net/11336/39121
identifier_str_mv Klinke, Sebastian; Zylberman, Vanesa; Vega, Daniel Roberto; Guimarães, Beatriz G.; Braden, Bradford C.; et al.; Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?; Elsevier; Journal Of Molecular Biology; 353; 1; 10-2005; 124-137
0022-2836
1089-8638
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S002228360500954X
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jmb.2005.08.017
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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