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作 者:Xiaoyan Zhao Hai Pang Shenglan Wang Weihong Zhou Keqian Yang Mark Bartlam
机构地区:[1]Laboratory of Structural Biology,Tsinghua University,Beijing 100084,China [2]Center for Microbial Metabolism and Metabolic Engineering,Institute of Microbiology,Chinese Academy of Sciences,Beijing 100101,China [3]Tianjin Key Laboratory of Protein Science,College of Life Sciences,Nankai University,Tianjin 300071,China
出 处:《Protein & Cell》2010年第8期771-779,共9页蛋白质与细胞(英文版)
基 金:supported by the National Natural Science Foundation of China(Grant Nos.30400259,30221003);the National Basic Research Program(973 Program)(Grant No.2007CB914301);the Tianjin Municipal Science and Technology Commission(Grant No.08SYSYTC00200).
摘 要: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-terminalα-helix,unpaired ligand-binding EF-hands and the lack of the extreme Cterminal 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.
关 键 词:calcium-binding protein crystal structure Streptomyces coelicolor calcium-mediated regulation EFhand
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