3UJG

Crystal structure of SnRK2.6 in complex with HAB1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.209 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases.

Soon, F.F.Ng, L.M.Zhou, X.E.West, G.M.Kovach, A.Tan, M.H.Suino-Powell, K.M.He, Y.Xu, Y.Chalmers, M.J.Brunzelle, J.S.Zhang, H.Yang, H.Jiang, H.Li, J.Yong, E.L.Cutler, S.Zhu, J.K.Griffin, P.R.Melcher, K.Xu, H.E.

(2012) Science 335: 85-88

  • DOI: https://doi.org/10.1126/science.1215106
  • Primary Citation of Related Structures:  
    3UJG, 3UJK, 3UJL

  • PubMed Abstract: 

    Abscisic acid (ABA) is an essential hormone for plants to survive environmental stresses. At the center of the ABA signaling network is a subfamily of type 2C protein phosphatases (PP2Cs), which form exclusive interactions with ABA receptors and subfamily 2 Snfl-related kinase (SnRK2s). Here, we report a SnRK2-PP2C complex structure, which reveals marked similarity in PP2C recognition by SnRK2 and ABA receptors. In the complex, the kinase activation loop docks into the active site of PP2C, while the conserved ABA-sensing tryptophan of PP2C inserts into the kinase catalytic cleft, thus mimicking receptor-PP2C interactions. These structural results provide a simple mechanism that directly couples ABA binding to SnRK2 kinase activation and highlight a new paradigm of kinase-phosphatase regulation through mutual packing of their catalytic sites.


  • Organizational Affiliation

    Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue NE, Grand Rapids, MI 49503, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Serine/threonine-protein kinase SRK2E361Arabidopsis thalianaMutation(s): 2 
Gene Names: SRK2EOST1SNRK2.6At4g33950F17I5.140
EC: 2.7.11.1
UniProt
Find proteins for Q940H6 (Arabidopsis thaliana)
Explore Q940H6 
Go to UniProtKB:  Q940H6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ940H6
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Protein phosphatase 2C 16350Arabidopsis thalianaMutation(s): 0 
Gene Names: HAB1P2C-HAAt1g72770F28P22.4
EC: 3.1.3.16
UniProt
Find proteins for Q9CAJ0 (Arabidopsis thaliana)
Explore Q9CAJ0 
Go to UniProtKB:  Q9CAJ0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9CAJ0
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.209 
  • Space Group: I 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 154.835α = 90
b = 154.835β = 90
c = 70.966γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction
HKL-2000data collection
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-02-15
    Type: Initial release
  • Version 1.1: 2024-02-28
    Changes: Data collection, Database references, Derived calculations