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dc.contributor.author
Fernandez, Ignacio
dc.contributor.author
Otero, Lisandro Horacio
dc.contributor.author
Klinke, Sebastian
dc.contributor.author
Carrica, Mariela del Carmen
dc.contributor.author
Goldbaum, Fernando Alberto
dc.date.available
2016-12-16T21:23:46Z
dc.date.issued
2015-10
dc.identifier.citation
Fernandez, Ignacio; Otero, Lisandro Horacio; Klinke, Sebastian; Carrica, Mariela del Carmen; Goldbaum, Fernando Alberto; Snapshots of conformational changes of NtrX receiver domain shed light into its signal transduction mechanism; Elsevier; Journal Of Molecular Biology; 427; 20; 10-2015; 3258-3272
dc.identifier.issn
0022-2836
dc.identifier.uri
http://hdl.handle.net/11336/9660
dc.description.abstract
Brucella abortus is an important pathogenic bacterium that has to overcome oxygen deficiency in order to achieve a successful infection. Previously, we proved that a two-component system formed by the histidine kinase NtrY and the response regulator NtrX is essential to achieve an adaptive response to low oxygen tension conditions. Even though the relevance of this signaling pathway has already been demonstrated in other microorganisms, its molecular activation mechanism has not yet been described in detail. In this article, we report the first crystal structures from different conformations of the NtrX receiver domain from B. abortus, and we propose a sequence of events to explain the structural rearrangements along the activation process. The analysis of the structures obtained in the presence of the phosphoryl group analog beryllofluoride led us to postulate that changes in the interface formed by the α4 helix and the β5 strand are important for the activation, producing a reorientation of the α5 helix. Also, a biochemical characterization of the NtrX receiver domain enzymatic activities was performed, describing its autophosphorylation and autodephosphorylation kinetics. Finally, the role of H85, an important residue, was addressed by site-directed mutagenesis. Overall, these results provide significant structural basis for understanding the response regulator activation in this bacterial two-component system.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Ntrx
dc.subject
Receiver Domain
dc.subject
Signal Transduction
dc.subject
Brucella
dc.subject.classification
Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Snapshots of conformational changes of NtrX receiver domain shed light into its signal transduction mechanism
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-12-16T17:27:15Z
dc.journal.volume
427
dc.journal.number
20
dc.journal.pagination
3258-3272
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Fernandez, Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina
dc.description.fil
Fil: Otero, Lisandro Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Plataforma Argentina de Biología Estructural y Metabolómica; Argentina
dc.description.fil
Fil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Plataforma Argentina de Biología Estructural y Metabolómica; Argentina
dc.description.fil
Fil: Carrica, Mariela del Carmen. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina
dc.description.fil
Fil: Goldbaum, Fernando Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Plataforma Argentina de Biología Estructural y Metabolómica; Argentina
dc.journal.title
Journal Of Molecular Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0022283615003502
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jmb.2015.06.010


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