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Publication Abstract from PubMed

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 alpha-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.

Structural basis for prokaryotic calcium-mediated regulation by a Streptomyces coelicolor calcium binding protein.,Zhao X, Pang H, Wang S, Zhou W, Yang K, Bartlam M Protein Cell. 2010 Aug;1(8):771-9. Epub 2010 Aug 28. PMID:21203918^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.