Structural basis for prokaryotic calcium-mediated regulation by a Streptomyces coelicolor calcium binding protein.
10.1007/s13238-010-0085-z
- Author:
Xiaoyan ZHAO
1
;
Hai PANG
;
Shenglan WANG
;
Weihong ZHOU
;
Keqian YANG
;
Mark BARTLAM
Author Information
1. Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Binding Sites;
Calcium;
physiology;
Calcium-Binding Proteins;
chemistry;
Crystallography, X-Ray;
EF Hand Motifs;
Molecular Sequence Data;
Protein Binding;
Protein Structure, Tertiary;
Sequence Alignment;
Sequence Homology, Amino Acid;
Streptomyces coelicolor;
Structural Homology, Protein;
Surface Properties
- From:
Protein & Cell
2010;1(8):771-779
- CountryChina
- Language:English
-
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.
