2VY2

Structure of LEAFY transcription factor from Arabidopsis thaliana in complex with DNA from AG-I promoter


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.262 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.232 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural Basis for Leafy Floral Switch Function and Similarity with Helix-Turn-Helix Proteins.

Hames, C.Ptchelkine, D.Grimm, C.Thevenon, E.Moyroud, E.Gerard, F.Martiel, J.L.Benlloch, R.Parcy, F.Muller, C.W.

(2008) EMBO J 27: 2628

  • DOI: https://doi.org/10.1038/emboj.2008.184
  • Primary Citation of Related Structures:  
    2VY1, 2VY2

  • PubMed Abstract: 

    The LEAFY (LFY) protein is a key regulator of flower development in angiosperms. Its gradually increased expression governs the sharp floral transition, and LFY subsequently controls the patterning of flower meristems by inducing the expression of floral homeotic genes. Despite a wealth of genetic data, how LFY functions at the molecular level is poorly understood. Here, we report crystal structures for the DNA-binding domain of Arabidopsis thaliana LFY bound to two target promoter elements. LFY adopts a novel seven-helix fold that binds DNA as a cooperative dimer, forming base-specific contacts in both the major and minor grooves. Cooperativity is mediated by two basic residues and plausibly accounts for LFY's effectiveness in triggering sharp developmental transitions. Our structure reveals an unexpected similarity between LFY and helix-turn-helix proteins, including homeodomain proteins known to regulate morphogenesis in higher eukaryotes. The appearance of flowering plants has been linked to the molecular evolution of LFY. Our study provides a unique framework to elucidate the molecular mechanisms underlying floral development and the evolutionary history of flowering plants.


  • Organizational Affiliation

    Laboratoire Physiologie Cellulaire Végétale, UMR5168, Centre National de la Recherche Scientifique, Commissariat à l'énergie atomique, Institut National de la Recherche Agronomique, Université Joseph Fourier, Grenoble, France.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN LEAFY194Arabidopsis thalianaMutation(s): 0 
UniProt
Find proteins for Q00958 (Arabidopsis thaliana)
Explore Q00958 
Go to UniProtKB:  Q00958
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ00958
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
5'-D(*AP*TP*TP*TP*AP*AP*TP*CP*CP*AP *AP*TP*GP*GP*TP*TP*AP*CP*AP*A)-3'B [auth W]20Arabidopsis thaliana
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.262 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.232 
  • Space Group: P 65 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 98.85α = 90
b = 98.85β = 90
c = 177.4γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
REFMACphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-09-23
    Type: Initial release
  • Version 1.1: 2012-01-18
    Changes: Data collection, Database references, Derived calculations, Non-polymer description, Other, Refinement description, Structure summary, Version format compliance
  • Version 1.2: 2023-12-13
    Changes: Data collection, Database references, Other, Refinement description