Here, we characterized the structure of the two-component regulatory system, LisR/LisK, in Listeria monocytogenes. To predict the structure of both proteins and the relationship between them, we employed several bioinformatic tools and databases. Based on our results, LisK protein is embedded in the...
- Autores:
-
Arenas Suarez, Nelson; Department of Biochemistry and Molecular Biology. University of Southern Denmark campusvej 55. 5230 Odense M, Denmark
Gutiérrez Escobar, Andrés; Grupo de Investigación GIBGA. Facultad de Medicina. Universidad de Ciencias Aplicadas y Ambientales. U.D.C.A.
Sánchez-Goméz, Myriam; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
Salazar, Luz Mary; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
Reyes Montaño, Edgar; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2013
- Institución:
- Pontificia Universidad Javeriana
- Repositorio:
- Repositorio Universidad Javeriana
- Idioma:
- eng
- OAI Identifier:
- oai:repository.javeriana.edu.co:10554/32009
- Acceso en línea:
- http://revistas.javeriana.edu.co/index.php/scientarium/article/view/4757
http://hdl.handle.net/10554/32009
- Palabra clave:
- Bioinformatics and Modeling
Listeria monocytogenes ; LisR/LisK; two-component regulatory systems; protein histidine kinase.
Proteínas
- Rights
- openAccess
- License
- Atribución-NoComercial-SinDerivadas 4.0 Internacional
| Summary: | Here, we characterized the structure of the two-component regulatory system, LisR/LisK, in Listeria monocytogenes. To predict the structure of both proteins and the relationship between them, we employed several bioinformatic tools and databases. Based on our results, LisK protein is embedded in the cell membrane and its modular composition (HAMP, histidine kinase and ATPase domains) is associated with its autophosphorylation (His-266). A stimulus-response likely determines the sequential signal propagation from the bacterial cell surface to its cytoplasmic components. According to our results, LisR is a cytoplasmic protein with a receptor domain (homologous to CheY) that comprises a phosphoacceptor residue (Asp-52) and a DNA-binding domain, which may allow the transmission of a specific transcriptional response. LisR/LisK has been experimentally characterized both biochemically and functionally in other Bacilli pathophysiology; our structure-function approach may facilitate the design of suitable inhibitors. |
|---|