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. 2010 Aug 28;1(8):771–779. doi: 10.1007/s13238-010-0085-z

Structural basis for prokaryotic calciummediated regulation by a Streptomyces coelicolor calcium binding protein

Xiaoyan Zhao 1, Hai Pang 1, Shenglan Wang 2, Weihong Zhou 3, Keqian Yang 2,✉, Mark Bartlam 3,✉
PMCID: PMC4875191  PMID: 21203918

Abstract

The important and diverse regulatory roles of Ca2+ 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.

Keywords: calcium-binding protein, crystal structure, Streptomyces coelicolor, calcium-mediated regulation, EF-hand

Footnotes

These authors contributed equally to the work.

Contributor Information

Keqian Yang, Email: yangkq@im.ac.cn.

Mark Bartlam, Email: bartlam@nankai.edu.cn.

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