5AAR

Structure of the ankyrin domain of an Arabidopsis Thaliana potassium channel


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.87 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.197 
  • R-Value Observed: 0.200 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Recognition and activation of the plant AKT1 potassium channel by the kinase CIPK23.

Sanchez-Barrena, M.J.Chaves-Sanjuan, A.Raddatz, N.Mendoza, I.Cortes, A.Gago, F.Gonzalez-Rubio, J.M.Benavente, J.L.Quintero, F.J.Pardo, J.M.Albert, A.

(2020) Plant Physiol 

  • DOI: https://doi.org/10.1104/pp.19.01084
  • Primary Citation of Related Structures:  
    5AAR

  • PubMed Abstract: 

    Plant growth largely depends on the maintenance of adequate intracellular levels of potassium (K + ). The families of 10 Calcineurin B-Like (CBL) calcium sensors and 26 CBL-Interacting Protein Kinases (CIPKs) of Arabidopsis ( Arabidopsis thaliana ) decode the calcium signals elicited by environmental inputs to regulate different ion channels and transporters involved in the control of K + fluxes by phosphorylation-dependent and -independent events. However, the detailed molecular mechanisms governing target specificity require investigation. Here, we show that the physical interaction between CIPK23 and the noncanonical ankyrin domain in the cytosolic side of the inward-rectifier K + channel AKT1 regulates kinase docking and channel activation. Point mutations on this domain specifically alter binding to CIPK23, enhancing or impairing the ability of CIPK23 to regulate channel activity. Our data demonstrate the relevance of this protein-protein interaction that contributes to the formation of a complex between CIPK23/CBL1 and AKT1 in the membrane for the proper regulation of K + transport.


  • Organizational Affiliation

    Departamento de Cristalografía y Biología Estructural, Instituto de Química Física "Rocasolano", Consejo Superior de Investigaciones Científicas, E-28006 Madrid, Spain.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
POTASSIUM CHANNEL AKT1185Arabidopsis thalianaMutation(s): 0 
UniProt
Find proteins for Q38998 (Arabidopsis thaliana)
Explore Q38998 
Go to UniProtKB:  Q38998
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ38998
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.87 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.197 
  • R-Value Observed: 0.200 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 34.921α = 90
b = 85.57β = 90
c = 65.989γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-08-24
    Type: Initial release
  • Version 1.1: 2020-04-08
    Changes: Database references, Other
  • Version 1.2: 2024-01-10
    Changes: Data collection, Database references, Derived calculations, Refinement description