Structural study for the novel regulation mechanism by calcium ion

钙离子新型调控机制的结构研究

• 批准号: 15570101
• 负责人: SHIMIZU Toshiyuki
• 金额: $ 2.37万
• 依托单位: Yokohama City University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 2003
• 资助国家: 日本
• 起止时间: 2003 至 2004
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-15570101/
• 关键词: CBL2; EF-hand; calcium; X-ray analysis; CIPK; calcineurin; plant; X線結晶構造解析; EFハンド; カルシウムセンサー

Calcium signaling mechanisms are widely employed by all eukaryotic organisms to regulate gene expression and a variety of cellular processes. In plants, many extracellular signals, such as light, drought, cold, salinity, stress factors, elicit changes in cellular calcium concentration. The calcium sensor protein often changes its conformation in a calcium-dependent manner and interacts with other signaling proteins to relay the signal. Several families of calcium sensor proteins have been identified in higher plants. Recently, novel calcium sensor proteins with EF-hand motifs from Arabidopsis thaliana have been identified, referred to as AtCBL(Arabidopsis thaliana calcineurin B-like protein). A family of SNF1 has been identified as targets for CBL proteins(7-9).These are serine-threonine protein kinases, referred to as AtCIPK(Arabidopsis thaliana CBL-interacting protein kinase), that form a novel family of proteins found so far only in plants.The crystal structure of AtCBL2 has been determined at 2.1A resolution. The protein forms a compact a-helical structure with two pairs of EF-hand motifs. The structure is similar in overall folding topology to the structures of calcineurin B and neuronal calcium sensor 1 , but differs significantly in local conformation. The two calcium ions are coordinated in the first and fourth EF-hand motifs, while the second and third EF-hand motifs are maintained in the open form by internal hydrogen bonding without coordination of calcium ions. Both a possible site and a possible mechanism for the target binding to AtCBL2 are discussed based on the three-dimensional structure.

钙信号传导机制被所有真核生物广泛用于调节基因表达和各种细胞过程。在植物中，许多细胞外信号，如光、干旱、寒冷、盐、胁迫因子，都会引起细胞内钙离子浓度的变化。钙传感器蛋白通常以钙依赖的方式改变其构象，并与其他信号蛋白相互作用以传递信号。在高等植物中已经鉴定出几个钙传感蛋白家族。近年来，在拟南芥中发现了一种新的具有EF-手结构的钙传感蛋白，称为AtCBL（Arabidopsis thaliana calcineurin B-like protein）。SNF 1家族已被鉴定为CBL蛋白的靶（7-9）。这些是丝氨酸-苏氨酸蛋白激酶，称为AtCIPK（拟南芥CBL相互作用蛋白激酶），形成迄今仅在植物中发现的新蛋白家族。AtCBL 2的晶体结构已在2.1A分辨率下确定。该蛋白形成一个紧凑的α-螺旋结构，具有两对EF-手形基序。该结构在整体折叠拓扑结构上类似于钙调磷酸酶B和神经元钙传感器1的结构，但在局部构象上显著不同。两个钙离子在第一和第四EF-手图案中配位，而第二和第三EF-手图案通过内部氢键保持开放形式，而没有钙离子的配位。根据其三维结构，讨论了靶分子与AtCBL 2结合的可能位点和可能机制。

项目成果

Nagae et al.: "Crystallization and preliminary X-ray characterization of novel calcium binding protein AtCBL2 from Arabidopsis thaliana"Acta Crystallogr.. D59. 1079-1080 (2003)

Nagae 等人：“来自拟南芥的新型钙结合蛋白 AtCBL2 的结晶和初步 X 射线表征”Acta Crystallogr.. D59。

Arita, et. al. Structural basis for Ca^<2+>-induced activation of human PAD4

有田等.

• 发表时间: 2004
• 期刊: Nat Struct Mol Biol 11
• 作者: Arita;et. al.
• 通讯作者: et. al.

カルシニューリンサブユニットB様蛋白質の結晶その製造方法、探索方法

钙调神经磷酸酶亚基B样蛋白晶体的制备及探索方法

• 发表时间: 2003

The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana

• DOI: 10.1074/jbc.m303630200
• 发表时间: 2003-10-24
• 期刊: JOURNAL OF BIOLOGICAL CHEMISTRY
• 影响因子: 4.8
• 作者: Nagae, M;Nozawa, A;Shimizu, T
• 通讯作者: Shimizu, T

Crystallographic characterization of the N-terminal domain of PEX1

PEX1 N 端结构域的晶体学表征

• 发表时间: 2004
• 期刊: Acta Crystallogr D60
• 作者: Shiozawa;K.;et. al.
• 通讯作者: et. al.