Structural basis for prokaryotic calcium-mediated regulation by a Streptomyces coelicolor calcium binding protein
Protein & Cell
; (12): 771-779, 2010.
Article
en En
| WPRIM
| ID: wpr-757442
Biblioteca responsable:
WPRO
ABSTRACT
The important and diverse regulatory roles of Ca(2+) in eukaryotes are conveyed by the EF-hand containing calmodulin superfamily. However, the calcium-regulatory proteins in prokaryotes are still poorly understood. In this study, we report the three-dimensional structure of the calcium-binding protein from Streptomyces coelicolor, named CabD, which shares low sequence homology with other known helix-loop-helix EF-hand proteins. The CabD structure should provide insights into the biological role of the prokaryotic calcium-binding proteins. The unusual structural features of CabD compared with prokaryotic EF-hand proteins and eukaryotic sarcoplasmic calcium-binding proteins, including the bending conformation of the first C-terminal α-helix, unpaired ligand-binding EF-hands and the lack of the extreme C-terminal loop region, suggest it may have a distinct and significant function in calcium-mediated bacterial physiological processes, and provide a structural basis for potential calcium-mediated regulatory roles in prokaryotes.
Texto completo:
1
Base de datos:
WPRIM
Asunto principal:
Fisiología
/
Unión Proteica
/
Propiedades de Superficie
/
Sitios de Unión
/
Proteínas de Unión al Calcio
/
Datos de Secuencia Molecular
/
Química
/
Calcio
/
Alineación de Secuencia
/
Secuencia de Aminoácidos
Idioma:
En
Revista:
Protein & Cell
Año:
2010
Tipo del documento:
Article