The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana
The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana
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DOI：
10.1074/jbc.m303630200
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发表时间：
2003-10-24
影响因子：
4.8
通讯作者：
Shimizu, T
中科院分区：
文献类型：
--
作者：
Nagae, M;Nozawa, A;Shimizu, T
拟南芥钙调神经磷酸酶B样蛋白（AtCBL 2）是最近在拟南芥中发现的钙调神经磷酸酶B样钙结合蛋白家族的一员。thaliana. AtCBL 2的晶体结构已在2.1埃分辨率下确定。该蛋白质形成一个紧凑的α-螺旋结构，具有两对EF-手基序。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。
Arabidopsis thaliana calcineurin B-like protein (AtCBL2) is a member of a recently identified family of calcineurin B-like calcium-binding proteins in A. thaliana. The crystal structure of AtCBL2 has been determined at 2.1 Angstrom resolution. The protein forms a compact alpha-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, whereas 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.