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Structures of Anabaena Calcium-binding Protein CcbP INSIGHTS INTO CA(2+) SIGNALING DURING HETEROCYST DIFFERENTIATION

文献类型：期刊论文

作者Hu, Yunfei1; Zhang, Xinxin1; Shi, Yunming2; Zhou, Yanfeng; Zhang, Wei2; Su, Xiao-Dong; Xia, Bin1,3,4; Zhao, Jindong1,2,3,5; Jin, Changwen1,2,4
刊名JOURNAL OF BIOLOGICAL CHEMISTRY
出版日期2011-04-08
卷号286期号:14页码:-
关键词DIPHTHERIA-TOXIN REPRESSOR TORSION ANGLE DYNAMICS EF-HAND PROTEINS NMR EXPERIMENTS NOE ASSIGNMENT SH3 DOMAINS HOMOLOGY SRC CYANOBACTERIA PROGRAMS
ISSN号0021-9258
通讯作者Zhao, JD, Peking Univ, Coll Life Sci, Beijing Nucl Magnet Resonance Ctr, Beijing 100871, Peoples R China ; jzhao@pku.edu.cn ; changwen@pku.edu.cn
中文摘要Ca2+-binding proteins play pivotal roles in both eukaryotic and prokaryotic cells. CcbP from cyanobacterium Anabaena sp. strain PCC 7120 is a major Ca2+-binding protein involved in heterocyst differentiation, a process that forms specialized nitrogen-fixing cells. The three-dimensional structures of both Ca2+-free and Ca2+-bound forms of CcbP are essential for elucidating the Ca2+-signaling mechanism. However, CcbP shares low sequence identity with proteins of known structures, and its Ca2+-binding sites remain unknown. Here, we report the solution structures of CcbP in both Ca2+-free and Ca2+-bound forms determined by nuclear magnetic resonance spectroscopy. CcbP adopts an overall new fold and contains two Ca2+-binding sites with distinct Ca2+-binding abilities. Mutation of Asp(38) at the stronger Ca2+-binding site of CcbP abolished its ability to regulate heterocyst formation in vivo. Surprisingly, the beta-barrel subdomain of CcbP, which does not participate in Ca2+-binding, topologically resembles the Src homology 3 (SH3) domain and might act as a protein-protein interaction module. Our results provide the structural basis of the unique Ca2+ signaling mechanism during heterocyst differentiation.
英文摘要Ca2+-binding proteins play pivotal roles in both eukaryotic and prokaryotic cells. CcbP from cyanobacterium Anabaena sp. strain PCC 7120 is a major Ca2+-binding protein involved in heterocyst differentiation, a process that forms specialized nitrogen-fixing cells. The three-dimensional structures of both Ca2+-free and Ca2+-bound forms of CcbP are essential for elucidating the Ca2+-signaling mechanism. However, CcbP shares low sequence identity with proteins of known structures, and its Ca2+-binding sites remain unknown. Here, we report the solution structures of CcbP in both Ca2+-free and Ca2+-bound forms determined by nuclear magnetic resonance spectroscopy. CcbP adopts an overall new fold and contains two Ca2+-binding sites with distinct Ca2+-binding abilities. Mutation of Asp(38) at the stronger Ca2+-binding site of CcbP abolished its ability to regulate heterocyst formation in vivo. Surprisingly, the beta-barrel subdomain of CcbP, which does not participate in Ca2+-binding, topologically resembles the Src homology 3 (SH3) domain and might act as a protein-protein interaction module. Our results provide the structural basis of the unique Ca2+ signaling mechanism during heterocyst differentiation.
WOS标题词Science & Technology ; Life Sciences & Biomedicine
学科主题Biochemistry & Molecular Biology
类目[WOS]Biochemistry & Molecular Biology
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]DIPHTHERIA-TOXIN REPRESSOR ; TORSION ANGLE DYNAMICS ; EF-HAND PROTEINS ; NMR EXPERIMENTS ; NOE ASSIGNMENT ; SH3 DOMAINS ; HOMOLOGY ; SRC ; CYANOBACTERIA ; PROGRAMS
收录类别SCI
资助信息National Natural Science Foundation [30325010, 30230040]; Ministry of Science and Technology of China [2006CB910203, 2006AA02A323]
语种英语
WOS记录号WOS:000289077500052
公开日期2011-06-30
源URL[http://ir.ihb.ac.cn/handle/342005/15672]  
专题水生生物研究所_水生生物分子与细胞生物学研究中心_期刊论文
作者单位1.Peking Univ, Coll Life Sci, Beijing Nucl Magnet Resonance Ctr, Beijing 100871, Peoples R China
2.Peking Univ, State Key Lab Plant & Prot Engn, Beijing 100871, Peoples R China
3.Peking Univ, Coll Chem & Mol Engn, Beijing 100871, Peoples R China
4.Peking Univ, Beijing Natl Lab Mol Sci, Beijing 100871, Peoples R China
5.Chinese Acad Sci, Inst Hydrobiol, Wuhan 430072, Hubei, Peoples R China
推荐引用方式
GB/T 7714		 Hu, Yunfei,Zhang, Xinxin,Shi, Yunming,et al. Structures of Anabaena Calcium-binding Protein CcbP INSIGHTS INTO CA(2+) SIGNALING DURING HETEROCYST DIFFERENTIATION[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2011,286(14):-.
APA Hu, Yunfei.,Zhang, Xinxin.,Shi, Yunming.,Zhou, Yanfeng.,Zhang, Wei.,...&Jin, Changwen.(2011).Structures of Anabaena Calcium-binding Protein CcbP INSIGHTS INTO CA(2+) SIGNALING DURING HETEROCYST DIFFERENTIATION.JOURNAL OF BIOLOGICAL CHEMISTRY,286(14),-.
MLA Hu, Yunfei,et al."Structures of Anabaena Calcium-binding Protein CcbP INSIGHTS INTO CA(2+) SIGNALING DURING HETEROCYST DIFFERENTIATION".JOURNAL OF BIOLOGICAL CHEMISTRY 286.14(2011):-.

入库方式： OAI收割

来源：水生生物研究所

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