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dc.contributor.author
Trajtenberg, Felipe
dc.contributor.author
Imelio, Juan A.
dc.contributor.author
Machado, Matías R.
dc.contributor.author
Larrieux, Nicole
dc.contributor.author
Marti, Marcelo Adrian
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dc.contributor.author
Obal, Gonzalo
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Mechaly, Ariel Edgardo
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dc.contributor.author
Buschiazzo, Alejandro
dc.date.available
2022-12-27T18:57:21Z
dc.date.issued
2016-12-12
dc.identifier.citation
Trajtenberg, Felipe; Imelio, Juan A.; Machado, Matías R.; Larrieux, Nicole; Marti, Marcelo Adrian; et al.; Regulation of signaling directionality revealed by 3D snapshots of a kinase: Regulator complex in action; eLife Sciences Publications Ltd; eLife; 5; 12-12-2016; 1-27
dc.identifier.issn
2050-084X
dc.identifier.uri
http://hdl.handle.net/11336/182605
dc.description.abstract
Two-component systems (TCS) are protein machineries that enable cells to respond to input signals. Histidine kinases (HK) are the sensory component, transferring information toward downstream response regulators (RR). HKs transfer phosphoryl groups to their specific RRs, but also dephosphorylate them, overall ensuring proper signaling. The mechanisms by which HKs discriminate between such disparate directions, are yet unknown. We now disclose crystal structures of the HK:RR complex DesK:DesR from Bacillus subtilis, comprising snapshots of the phosphotransfer and the dephosphorylation reactions. The HK dictates the reactional outcome through conformational rearrangements that include the reactive histidine. The phosphotransfer center is asymmetric, poised for dissociative nucleophilic substitution. The structural bases of HK phosphatase/phosphotransferase control are uncovered, and the unexpected discovery of a dissociative reactional center, sheds light on the evolution of TCS phosphotransfer reversibility. Our findings should be applicable to a broad range of signaling systems and instrumental in synthetic TCS rewiring.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
eLife Sciences Publications Ltd
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
B. subtilis
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E. coli
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Allosteric control of protein function
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Biophysics
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Regulation of signaling directionality revealed by 3D snapshots of a kinase: Regulator complex in action
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2022-12-27T11:10:39Z
dc.identifier.eissn
2050-084X
dc.journal.volume
5
dc.journal.pagination
1-27
dc.journal.pais
Reino Unido
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dc.description.fil
Fil: Trajtenberg, Felipe. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Imelio, Juan A.. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Machado, Matías R.. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Larrieux, Nicole. Instituto Pasteur de Montevideo; Uruguay
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Fil: Marti, Marcelo Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
dc.description.fil
Fil: Obal, Gonzalo. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Mechaly, Ariel Edgardo. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Buschiazzo, Alejandro. Instituto Pasteur de Montevideo; Uruguay. Institut Pasteur de Paris.; Francia
dc.journal.title
eLife
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://elifesciences.org/articles/21422
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.7554/eLife.21422
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