A bacterial calcium-binding protein homologous to calmodulin

Many of the effects of calcium ions in eukaryotic cells are mediated by calcium-binding regulatory proteins such as calmodulin, in which each calcium-binding site has a distinctive helix-loop-helix conformation termed the EF hand. Protein S from the spore coat of the Gram-negative bacterium Myxococc...

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Bibliographic Details
Published in:Nature (London) 1987-09, Vol.329 (6134), p.84-85
Main Authors: Swan, David G, Hale, Richard S, Dhillon, Namrita, Leadlay, Peter F
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacteria
Biochemistry
Calcium
calcium-binding protein
Calcium-Binding Proteins - genetics
calmodulin
Calmodulin - genetics
Cloning
DNA
Genes
Humans
Ions
nucleotide sequence
Protein Conformation
Proteins
Sequence Homology, Nucleic Acid
Streptomyces - genetics
Streptomyces erythraeus
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Summary:Many of the effects of calcium ions in eukaryotic cells are mediated by calcium-binding regulatory proteins such as calmodulin, in which each calcium-binding site has a distinctive helix-loop-helix conformation termed the EF hand. Protein S from the spore coat of the Gram-negative bacterium Myxococcus xanthus has been shown to resemble calmodulin in its internally-duplicated structure and ability to bind calcium. However, it has a beta-sheet secondary structure rather than the helix-loop-helix arrangement of the eukaryotic proteins. We have determined the complete amino-acid sequence of a calcium-binding protein from the Gram-positive bacterium "Streptomyces erythraeus" by cloning and sequencing the corresponding gene. It contains four EF-hand motifs bearing remarkable sequence similarity to the calcium-binding sites in calmodulin. This implies that the EF-hand super-family may have evolved from ancient proteins present in prokaryotes.
ISSN:0028-0836
1476-4687
DOI:10.1038/329084a0