Preliminary crystallographic analysis of the ankyrin-repeat domain of Arabidopsis thaliana AKT1: Identification of the domain boundaries for protein crystallization
Articolo
Data di Pubblicazione:
2014
Citazione:
Preliminary crystallographic analysis of the ankyrin-repeat domain of Arabidopsis thaliana AKT1: Identification of the domain boundaries for protein crystallization / A. Chaves-Sanjuan, M.J. Sanchez-Barrena, J.M. Gonzalez-Rubio, A. Albert. - In: ACTA CRYSTALLOGRAPHICA. SECTION F, STRUCTURAL BIOLOGY COMMUNICATIONS. - ISSN 2053-230X. - 70:4(2014 Apr), pp. 509-512. [10.1107/S2053230X14005093]
Abstract:
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. © 2014 International Union of Crystallography All rights reserved.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
AKT1; Arabidopsis thaliana; Arabidopsis; Arabidopsis Proteins; Crystallization; Crystallography, X-Ray; Potassium Channels; Ankyrin Repeat
Elenco autori:
A. Chaves-Sanjuan, M.J. Sanchez-Barrena, J.M. Gonzalez-Rubio, A. Albert
Link alla scheda completa:
Link al Full Text: