Structural basis for prokaryotic calcium-mediated regulation by a Streptomyces coelicolor calcium binding protein
Protein & Cell
;
(12): 771-779, 2010.
Artigo
em Inglês
| WPRIM
| ID: wpr-757442
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:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Fisiologia
/
Ligação Proteica
/
Propriedades de Superfície
/
Sítios de Ligação
/
Proteínas de Ligação ao Cálcio
/
Dados de Sequência Molecular
/
Química
/
Cálcio
/
Alinhamento de Sequência
/
Sequência de Aminoácidos
Idioma:
Inglês
Revista:
Protein & Cell
Ano de publicação:
2010
Tipo de documento:
Artigo
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