1EGW

CRYSTAL STRUCTURE OF MEF2A CORE BOUND TO DNA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.206 

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This is version 1.4 of the entry. See complete history


Literature

Crystal structure of MEF2A core bound to DNA at 1.5 A resolution.

Santelli, E.Richmond, T.J.

(2000) J Mol Biol 297: 437-449

  • DOI: https://doi.org/10.1006/jmbi.2000.3568
  • Primary Citation of Related Structures:  
    1EGW

  • PubMed Abstract: 

    Members of the myocyte enhancer factor-2 (MEF2) family of transcription factors bind to and activate transcription through A+T-rich DNA sequences found primarily, but not exclusively, in the promoters of muscle-specific genes. Their importance has been established for myogenic development and in activation of the immediate-early gene, c-jun, and recently further functional roles in the immune system have emerged. The MEF2 factors belong to the MADS-box superfamily, sharing homology in a 58 amino acid domain that mediates DNA binding and dimerization. The structures of two MADS-box proteins, SRF and MCM1, bound to their cognate DNA have been previously reported and shown to share extensive similarity in their mode of DNA binding. We have solved the structure of MEF2A 2-78 bound to its DNA consensus sequence at 1.5 A resolution. It reveals how the absence of amino acids N-terminal to the MADS-box contributes to the DNA binding properties of MEF2 proteins and shows that the MEF domain C-terminal to the MADS-box adopts a conformation considerably different from the same region in SRF and MCM1.


  • Organizational Affiliation

    Institut für Molekularbiologie und Biophysik, ETH Zurich, Zürich, CH, Switzerland.


Macromolecules

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
MADS BOX TRANSCRIPTION ENHANCER FACTOR 2, POLYPEPTIDE AE [auth A],
F [auth B],
G [auth C],
H [auth D]
77Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for Q02078 (Homo sapiens)
Explore Q02078 
Go to UniProtKB:  Q02078
PHAROS:  Q02078
GTEx:  ENSG00000068305 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ02078
Sequence Annotations
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
DNA (5'-D(*AP*AP*AP*GP*CP*TP*AP*TP*TP*AP*TP*TP*AP*GP*CP*TP*T)-3')A [auth E],
D [auth H]
17N/A
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
DNA (5'-D(*TP*AP*AP*GP*CP*TP*AP*AP*TP*AP*AP*TP*AP*GP*CP*TP*T)-3')B [auth F],
C [auth G]
17N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.206 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 41.371α = 115.18
b = 60.696β = 89.99
c = 63.987γ = 90
Software Package:
Software NamePurpose
AMoREphasing
MLPHAREphasing
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-03-20
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-04-04
    Changes: Data collection
  • Version 1.4: 2024-02-07
    Changes: Data collection, Database references