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dc.contributor.author
Lisa, María Natalia
dc.contributor.author
Wagner, Tristan
dc.contributor.author
Alexandre, Matthieu
dc.contributor.author
Barilone, Nathalie
dc.contributor.author
Raynal, Bertrand
dc.contributor.author
Alzari, Pedro M.
dc.contributor.author
Bellinzoni, Marco
dc.date.available
2018-12-06T19:30:24Z
dc.date.issued
2017-02
dc.identifier.citation
Lisa, María Natalia; Wagner, Tristan; Alexandre, Matthieu; Barilone, Nathalie; Raynal, Bertrand; et al.; The crystal structure of PknI from Mycobacterium tuberculosis shows an inactive, pseudokinase-like conformation; Wiley Blackwell Publishing, Inc; Febs Journal; 284; 4; 2-2017; 602-614
dc.identifier.issn
1742-464X
dc.identifier.uri
http://hdl.handle.net/11336/66031
dc.description.abstract
Eukaryotic-like Ser/Thr protein kinases (ePKs) have been identified in many bacterial species, where they are known to mediate signalling mechanisms that share several features with their eukaryotic counterparts. In Mycobacterium tuberculosis, PknI is one of the 11 predicted ePKs and it has been related to bacterial virulence. In order to better understand the molecular basis of its role in mycobacterial signalling, we solved the crystal structure of the PknI cytoplasmic domain. We found that even though PknI possesses most conserved elements characteristic of Hanks-type kinases, it is degraded in several motifs that are essential for the ePKs catalytic activity. Most notably, PknI presents a remarkably short activation segment lacking a peptide–substrate binding site. Consistent with this observation and similar to earlier findings for eukaryotic pseudokinases, no kinase activity was detected for the catalytic domain of PknI, against different substrates and in various experimental conditions. Based on these results, we conclude that PknI may rely on unconventional mechanism(s) for kinase activity and/or it could play alternative role(s) in mycobacterial signalling. Database: Atomic coordinates and structure factors for the catalytic domain of M. tuberculosis PknI are in the Protein Data Bank under the accession codes 5M06 (wild-type PknI + ADP), 5M07 (PknI_C20A), 5M08 (PknI_C20A_R136A) and 5M09 (PknI_C20A_R136N).
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley Blackwell Publishing, Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Activation Segment
dc.subject
Ser/Thr Kinase
dc.subject
Signal Transduction
dc.subject
X-Ray Crystallography
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
The crystal structure of PknI from Mycobacterium tuberculosis shows an inactive, pseudokinase-like conformation
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-11-02T15:13:58Z
dc.journal.volume
284
dc.journal.number
4
dc.journal.pagination
602-614
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Lisa, María Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina. Universite de Paris V; Francia. Instituto Pasteur; Francia
dc.description.fil
Fil: Wagner, Tristan. Instituto Pasteur; Francia. Universite de Paris V; Francia
dc.description.fil
Fil: Alexandre, Matthieu. Instituto Pasteur; Francia. Universite de Paris V; Francia
dc.description.fil
Fil: Barilone, Nathalie. Instituto Pasteur; Francia. Universite de Paris V; Francia
dc.description.fil
Fil: Raynal, Bertrand. Instituto Pasteur; Francia. Universite de Paris V; Francia
dc.description.fil
Fil: Alzari, Pedro M.. Instituto Pasteur; Francia. Universite de Paris V; Francia
dc.description.fil
Fil: Bellinzoni, Marco. Instituto Pasteur; Francia. Universite de Paris V; Francia
dc.journal.title
Febs Journal
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/febs.14003/abstract
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1111/febs.14003
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