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Preliminary crystallographic analysis of the ankyrin‐repeat domain of Arabidopsis thaliana AKT1: identification of the domain boundaries for protein crystallization
Author(s) -
ChavesSanjuán Antonio,
SánchezBarrena María José,
GonzálezRubio Juana María,
Albert Armando
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14005093
Subject(s) - ankyrin repeat , crystallization , akt1 , arabidopsis thaliana , crystallography , domain (mathematical analysis) , potassium , chemistry , biophysics , biology , biochemistry , gene , signal transduction , mutant , mathematical analysis , mathematics , organic chemistry , pi3k/akt/mtor pathway
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 P 2 1 2 1 2, with unit‐cell parameters a = 34.83, b = 65.89, c = 85.44 Å, and diffracted to 1.98 Å resolution.