4JYM

crystal Structure of KAI2 in complex with 3-methyl-2H-furo[2,3-c]pyran-2-one


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.35 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.183 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Smoke-derived karrikin perception by the alpha/beta-hydrolase KAI2 from Arabidopsis.

Guo, Y.Zheng, Z.La Clair, J.J.Chory, J.Noel, J.P.

(2013) Proc Natl Acad Sci U S A 110: 8284-8289

  • DOI: https://doi.org/10.1073/pnas.1306265110
  • Primary Citation of Related Structures:  
    4JYM, 4JYP

  • PubMed Abstract: 

    Genetic studies in Arabidopsis implicate an α/β-hydrolase, KARRIKIN-INSENSITIVE 2 (KAI2) as a receptor for karrikins, germination-promoting butenolide small molecules found in the smoke of burned plants. However, direct biochemical evidence for the interaction between KAI2 and karrikin and for the mechanism of downstream signaling by a KAI2-karrikin complex remain elusive. We report crystallographic analyses and ligand-binding experiments for KAI2 recognition of karrikins. The karrikin-1 (KAR1) ligand sits in the opening to the active site abutting a helical domain insert but distal from the canonical catalytic triad (Ser95-His246-Asp217) of α/β-hydrolases, consistent with the lack of detectable hydrolytic activity by purified KAI2. The closest approach of KAR1 to Ser95-His246-Asp217 is 3.8 Å from His246. Six aromatic side chains, including His246, encapsulate KAR1 through geometrically defined aromatic-aromatic interactions. KAR1 binding induces a conformational change in KAI2 at the active site entrance. A crevice of hydrophobic residues linking the polar edge of KAR1 and the helical domain insert suggests that KAI2-KAR1 creates a contiguous interface for binding signaling partners in a ligand-dependent manner.


  • Organizational Affiliation

    Jack H. Skirball Center for Chemical Biology and Proteomics, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hydrolase, alpha/beta fold family protein
A, B
270Arabidopsis thalianaMutation(s): 0 
Gene Names: F6G17.120AT4g37470
UniProt
Find proteins for Q9SZU7 (Arabidopsis thaliana)
Explore Q9SZU7 
Go to UniProtKB:  Q9SZU7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9SZU7
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
KKN
Query on KKN

Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]
3-methyl-2H-furo[2,3-c]pyran-2-one
C8 H6 O3
JUTMAMXOAOYKHT-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
KKN PDBBind:  4JYM Kd: 9050 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.35 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.183 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.95α = 90.04
b = 53.2β = 90.04
c = 55.76γ = 116.03
Software Package:
Software NamePurpose
SCALAdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction
BOSdata collection
MOSFLMdata reduction

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-05-08
    Type: Initial release
  • Version 1.1: 2013-06-19
    Changes: Database references
  • Version 1.2: 2019-08-28
    Changes: Advisory, Data collection, Refinement description, Structure summary
  • Version 1.3: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description