4AWL

The NF-Y transcription factor is structurally and functionally a sequence specific histone


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.08 Å
  • R-Value Free: 0.250 
  • R-Value Work: 0.191 
  • R-Value Observed: 0.194 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Sequence-Specific Transcription Factor NF-Y Displays Histone-Like DNA Binding and H2B-Like Ubiquitination.

Nardini, M.Gnesutta, N.Donati, G.Gatta, R.Forni, C.Fossati, A.Vonrhein, C.Moras, D.Romier, C.Bolognesi, M.Mantovani, R.

(2013) Cell 152: 132

  • DOI: https://doi.org/10.1016/j.cell.2012.11.047
  • Primary Citation of Related Structures:  
    4AWL

  • PubMed Abstract: 

    The sequence-specific transcription factor NF-Y binds the CCAAT box, one of the sequence elements most frequently found in eukaryotic promoters. NF-Y is composed of the NF-YA and NF-YB/NF-YC subunits, the latter two hosting histone-fold domains (HFDs). The crystal structure of NF-Y bound to a 25 bp CCAAT oligonucleotide shows that the HFD dimer binds to the DNA sugar-phosphate backbone, mimicking the nucleosome H2A/H2B-DNA assembly. NF-YA both binds to NF-YB/NF-YC and inserts an α helix deeply into the DNA minor groove, providing sequence-specific contacts to the CCAAT box. Structural considerations and mutational data indicate that NF-YB ubiquitination at Lys138 precedes and is equivalent to H2B Lys120 monoubiquitination, important in transcriptional activation. Thus, NF-Y is a sequence-specific transcription factor with nucleosome-like properties of nonspecific DNA binding and helps establish permissive chromatin modifications at CCAAT promoters. Our findings suggest that other HFD-containing proteins may function in similar ways.


  • Organizational Affiliation

    Dipartimento di BioScienze, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy.


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT ALPHA78Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P23511 (Homo sapiens)
Explore P23511 
Go to UniProtKB:  P23511
PHAROS:  P23511
GTEx:  ENSG00000001167 
Entity Groups  
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UniProt GroupP23511
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT BETA94Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P25208 (Homo sapiens)
Explore P25208 
Go to UniProtKB:  P25208
PHAROS:  P25208
GTEx:  ENSG00000120837 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP25208
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
NUCLEAR TRANSCRIPTION FACTOR Y SUBUNIT GAMMA94Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for Q13952 (Homo sapiens)
Explore Q13952 
Go to UniProtKB:  Q13952
PHAROS:  Q13952
GTEx:  ENSG00000066136 
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UniProt GroupQ13952
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  • Reference Sequence

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Entity ID: 4
MoleculeChains LengthOrganismImage
HSP70 PROMOTER FRAGMENTD [auth I]25Homo sapiens
Sequence Annotations
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  • Reference Sequence

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Entity ID: 5
MoleculeChains LengthOrganismImage
HSP70 PROMOTER FRAGMENTE [auth J]25Homo sapiens
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.08 Å
  • R-Value Free: 0.250 
  • R-Value Work: 0.191 
  • R-Value Observed: 0.194 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 54.7α = 90
b = 62.56β = 90
c = 139.68γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-01-30
    Type: Initial release
  • Version 1.1: 2019-05-08
    Changes: Data collection, Experimental preparation, Other
  • Version 1.2: 2023-12-20
    Changes: Data collection, Database references, Other, Refinement description