7SNU

Crystal structure of ShHTL7 from Striga hermonthica in complex with strigolactone antagonist RG6


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.46 Å
  • R-Value Free: 0.162 
  • R-Value Work: 0.128 
  • R-Value Observed: 0.129 

Starting Model: experimental
View more details

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

A novel strigolactone receptor antagonist provides insights into the structural inhibition, conditioning, and germination of the crop parasite Striga.

Arellano-Saab, A.McErlean, C.S.P.Lumba, S.Savchenko, A.Stogios, P.J.McCourt, P.

(2022) J Biol Chem 298: 101734-101734

  • DOI: https://doi.org/10.1016/j.jbc.2022.101734
  • Primary Citation of Related Structures:  
    7SNU

  • PubMed Abstract: 

    Crop parasites of the Striga genera are a major biological deterrent to food security in Africa and are one of the largest obstacles to poverty alleviation on the continent. Striga seeds germinate by sensing small-molecule hormones, strigolactones (SLs), that emanate from host roots. Although SL receptors (Striga hermonthica HYPOSENSITIVE TO LIGHT [ShHTL]) have been identified, discerning their function has been difficult because these parasites cannot be easily grown under laboratory conditions. Moreover, many Striga species are obligate outcrossers that are not transformable, hence not amenable to genetic analysis. By combining phenotypic screening with ShHTL structural information and hybrid drug discovery methods, we discovered a potent SL perception inhibitor for Striga, dormirazine (DOZ). Structural analysis of this piperazine-based antagonist reveals a novel binding mechanism, distinct from that of known SLs, blocking access of the hormone to its receptor. Furthermore, DOZ reduces the flexibility of protein-protein interaction domains important for receptor signaling to downstream partners. In planta, we show, via temporal additions of DOZ, that SL receptors are required at a specific time during seed conditioning. This conditioning is essential to prime seed germination at the right time; thus, this SL-sensitive stage appears to be critical for adequate receptor signaling. Aside from uncovering a function for ShHTL during seed conditioning, these results suggest that future Ag-Biotech Solutions to Striga infestations will need to carefully time the application of antagonists to exploit receptor availability and outcompete natural SLs, critical elements for successful parasitic plant invasions.


  • Organizational Affiliation

    Department of Cell and Systems Biology, University of Toronto, Toronto, Canada; Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hyposensitive to light 7272Striga hermonthicaMutation(s): 0 
UniProt
Find proteins for A0A0M3PNA2 (Striga hermonthica)
Explore A0A0M3PNA2 
Go to UniProtKB:  A0A0M3PNA2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0M3PNA2
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 5 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
HFJ (Subject of Investigation/LOI)
Query on HFJ

Download Ideal Coordinates CCD File 
K [auth A]2-{(2S)-1-[(4-ethoxyphenyl)methyl]-4-[(2E)-3-(4-methoxyphenyl)prop-2-en-1-yl]piperazin-2-yl}ethan-1-ol
C25 H34 N2 O3
MBXADFLSFSJJOZ-OIUIXCLQSA-N
GOL
Query on GOL

Download Ideal Coordinates CCD File 
B [auth A],
C [auth A]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
IMD
Query on IMD

Download Ideal Coordinates CCD File 
J [auth A]IMIDAZOLE
C3 H5 N2
RAXXELZNTBOGNW-UHFFFAOYSA-O
ACT
Query on ACT

Download Ideal Coordinates CCD File 
D [auth A],
E [auth A],
F [auth A],
G [auth A],
H [auth A]
ACETATE ION
C2 H3 O2
QTBSBXVTEAMEQO-UHFFFAOYSA-M
MG
Query on MG

Download Ideal Coordinates CCD File 
I [auth A]MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.46 Å
  • R-Value Free: 0.162 
  • R-Value Work: 0.128 
  • R-Value Observed: 0.129 
  • Space Group: P 65
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 96.216α = 90
b = 96.216β = 90
c = 69.358γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling
PHENIXphasing
PHENIXmodel building
Cootmodel building

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Natural Sciences and Engineering Research Council (NSERC, Canada)06752
Natural Sciences and Engineering Research Council (NSERC, Canada)507992
Natural Sciences and Engineering Research Council (NSERC, Canada)00356
Other governmentNFRFE-2018-00118
Natural Sciences and Engineering Research Council (NSERC, Canada)04298
Consejo Nacional de Ciencia y Tecnologia (CONACYT)--

Revision History  (Full details and data files)

  • Version 1.0: 2022-07-06
    Type: Initial release
  • Version 1.1: 2023-10-18
    Changes: Data collection, Refinement description