4UDE

An oligomerization domain confers pioneer properties to the LEAFY master floral regulator


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.190 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

A Sam Oligomerization Domain Shapes the Genomic Binding Landscape of the Leafy Transcription Factor

Sayou, C.Nanao, M.H.Jamin, M.Pose, D.Thevenon, E.Gregoire, L.Tichtinsky, G.Denay, G.Ott, F.Peirats Llobet, M.Schmid, M.Dumas, R.Parcy, F.

(2016) Nat Commun 7: 11222

  • DOI: https://doi.org/10.1038/ncomms11222
  • Primary Citation of Related Structures:  
    4UDE

  • PubMed Abstract: 

    Deciphering the mechanisms directing transcription factors (TFs) to specific genome regions is essential to understand and predict transcriptional regulation. TFs recognize short DNA motifs primarily through their DNA-binding domain. Some TFs also possess an oligomerization domain suspected to potentiate DNA binding but for which the genome-wide influence remains poorly understood. Here we focus on the LEAFY transcription factor, a master regulator of flower development in angiosperms. We have determined the crystal structure of its conserved amino-terminal domain, revealing an unanticipated Sterile Alpha Motif oligomerization domain. We show that this domain is essential to LEAFY floral function. Moreover, combined biochemical and genome-wide assays suggest that oligomerization is required for LEAFY to access regions with low-affinity binding sites or closed chromatin. This finding shows that domains that do not directly contact DNA can nevertheless have a profound impact on the DNA binding landscape of a TF.


  • Organizational Affiliation

    Laboratoire de Physiologie Cellulaire et Végétale, Université Grenoble Alpes, CNRS UMR5168, CEA/DRF/BIG, INRA UMR 1417, 17, avenue des Martyrs, 38054 Grenoble, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GINLFY PROTEIN
A, B
110Ginkgo bilobaMutation(s): 0 
UniProt
Find proteins for Q9LLY6 (Ginkgo biloba)
Explore Q9LLY6 
Go to UniProtKB:  Q9LLY6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9LLY6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.190 
  • Space Group: P 65
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.095α = 90
b = 81.095β = 90
c = 78.493γ = 120
Software Package:
Software NamePurpose
BUSTERrefinement
XDSdata reduction
XSCALEdata scaling
SHELXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-03-02
    Type: Initial release
  • Version 1.1: 2016-03-30
    Changes: Database references, Structure summary
  • Version 1.2: 2016-05-04
    Changes: Database references