Structural basis for prokaryotic calcium-mediated regulation by a Streptomyces coelicolor calcium binding protein
Protein & Cell
;
(12): 771-779, 2010.
Article
in English
| 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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Physiology
/
Protein Binding
/
Surface Properties
/
Binding Sites
/
Calcium-Binding Proteins
/
Molecular Sequence Data
/
Chemistry
/
Calcium
/
Sequence Alignment
/
Amino Acid Sequence
Language:
English
Journal:
Protein & Cell
Year:
2010
Type:
Article
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