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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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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)