Chaves-Sanjuán Antonio, Sánchez-Barrena María José, González-Rubio Juana María, Albert Armando
Departamento de Cristalografía y Biología Estructural, Instituto de Química-Física `Rocasolano', CSIC, Serrano 119, 28006 Madrid, Spain.
Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):509-12. doi: 10.1107/S2053230X14005093. Epub 2014 Mar 25.
The Arabidopsis thaliana K(+) transporter 1 (AKT1) participates in the maintenance of an adequate cell potassium (K(+)) concentration. The CBL-interacting protein kinase 23 (CIPK23) activates AKT1 for K(+) uptake under low-K(+) conditions. This process is mediated by the interaction between the cytosolic ankyrin-repeat (AR) domain of AKT1 and the kinase domain of CIPK23. However, the precise boundaries of the AR domain and the residues responsible for the interaction are still unknown. Here, the optimization procedure to obtain an AR domain construct suitable for crystallization and the preliminary crystallographic analysis of the obtained crystals are reported. The crystals belonged to space group P21212, with unit-cell parameters a = 34.83, b = 65.89, c = 85.44 Å, and diffracted to 1.98 Å resolution.
拟南芥钾离子转运体1（AKT1）参与维持细胞内适当的钾（K⁺）浓度。CBL相互作用蛋白激酶23（CIPK23）在低钾条件下激活AKT1以促进钾吸收。这一过程由AKT1胞质锚蛋白重复（AR）结构域与CIPK23激酶结构域之间的相互作用介导。然而，AR结构域的精确边界以及负责相互作用的残基仍然未知。在此，报道了获得适合结晶的AR结构域构建体的优化程序以及所得晶体的初步晶体学分析。晶体属于空间群P21212，晶胞参数a = 34.83、b = 65.89、c = 85.44 Å，衍射分辨率为1.98 Å。
