5NWK

14-3-3c in complex with CPP and fusicoccin


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.286 
  • R-Value Work: 0.229 
  • R-Value Observed: 0.231 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Fusicoccin Activates KAT1 Channels by Stabilizing Their Interaction with 14-3-3 Proteins.

Saponaro, A.Porro, A.Chaves-Sanjuan, A.Nardini, M.Rauh, O.Thiel, G.Moroni, A.

(2017) Plant Cell 29: 2570-2580

  • DOI: https://doi.org/10.1105/tpc.17.00375
  • Primary Citation of Related Structures:  
    5NWI, 5NWJ, 5NWK

  • PubMed Abstract: 

    Plants acquire potassium (K + ) ions for cell growth and movement via regulated diffusion through K + channels. Here, we present crystallographic and functional data showing that the K + inward rectifier KAT1 (K + Arabidopsis thaliana 1) channel is regulated by 14-3-3 proteins and further modulated by the phytotoxin fusicoccin, in analogy to the H + -ATPase. We identified a 14-3-3 mode III binding site at the very C terminus of KAT1 and cocrystallized it with tobacco ( Nicotiana tabacum ) 14-3-3 proteins to describe the protein complex at atomic detail. Validation of this interaction by electrophysiology shows that 14-3-3 binding augments KAT1 conductance by increasing the maximal current and by positively shifting the voltage dependency of gating. Fusicoccin potentiates the 14-3-3 effect on KAT1 activity by stabilizing their interaction. Crystal structure of the ternary complex reveals a noncanonical binding site for the toxin that adopts a novel conformation. The structural insights underscore the adaptability of fusicoccin, predicting more potential targets than so far anticipated. The data further advocate a common mechanism of regulation of the proton pump and a potassium channel, two essential elements in K + uptake in plant cells.


  • Organizational Affiliation

    Department of Biosciences, University of Milan, 20133 Milan, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
14-3-3 c-1 protein262Nicotiana tabacumMutation(s): 0 
Gene Names: 14-3-3 c-1LOC107777576Nt14-3-3omega2
UniProt
Find proteins for P93343 (Nicotiana tabacum)
Explore P93343 
Go to UniProtKB:  P93343
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP93343
Sequence Annotations
Expand
  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Potassium channel KAT15Arabidopsis thalianaMutation(s): 0 
UniProt
Find proteins for Q39128 (Arabidopsis thaliana)
Explore Q39128 
Go to UniProtKB:  Q39128
Entity Groups  
UniProt GroupQ39128
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
SEP
Query on SEP
B [auth P]
D [auth Q]
F [auth R]
H [auth S]
J [auth T]
B [auth P],
D [auth Q],
F [auth R],
H [auth S],
J [auth T],
L [auth U],
N [auth V],
P [auth W]
L-PEPTIDE LINKINGC3 H8 N O6 PSER
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.286 
  • R-Value Work: 0.229 
  • R-Value Observed: 0.231 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 99.806α = 90
b = 165.661β = 90
c = 170.552γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-11-22
    Type: Initial release
  • Version 1.1: 2024-01-17
    Changes: Data collection, Database references, Refinement description