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dc.contributor.author
Klinke, Sebastian
dc.contributor.author
Zylberman, Vanesa
dc.contributor.author
Vega, Daniel Roberto
dc.contributor.author
Guimarães, Beatriz G.
dc.contributor.author
Braden, Bradford C.
dc.contributor.author
Goldbaum, Fernando Alberto
dc.date.available
2018-03-16T19:09:42Z
dc.date.issued
2005-10
dc.identifier.citation
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
dc.identifier.issn
0022-2836
dc.identifier.uri
http://hdl.handle.net/11336/39121
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
6,7-Dimethyl-8-Ribityllumazine Synthase
dc.subject
Brucella Spp.
dc.subject
Quaternary Arrangement
dc.subject
Riboflavin Biosynthesis
dc.subject
X-Ray Crystallography
dc.subject.classification
Inmunología
dc.subject.classification
Medicina Básica
dc.subject.classification
CIENCIAS MÉDICAS Y DE LA SALUD
dc.title
Crystallographic studies on decameric Brucella spp. lumazine synthase: A novel quaternary arrangement evolved for a new function?
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-15T15:22:37Z
dc.identifier.eissn
1089-8638
dc.journal.volume
353
dc.journal.number
1
dc.journal.pagination
124-137
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
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
dc.description.fil
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
dc.description.fil
Fil: Vega, Daniel Roberto. Comisión Nacional de Energía Atómica; Argentina
dc.description.fil
Fil: Guimarães, Beatriz G.. Laboratorio Nacional de Luz Sincrotron; Brasil
dc.description.fil
Fil: Braden, Bradford C.. Bowie State University; Estados Unidos
dc.description.fil
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
dc.journal.title
Journal Of Molecular Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S002228360500954X
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jmb.2005.08.017


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