3MLP: Early B-cell Factor 1 (ebf1) Bound To Dna

Early B-cell factor 1 (Ebf1) is a key transcriptional determinant of B-lymphocyte differentiation whose DNA-binding domain has no sequence similarity to other transcription factor families. Here we report the crystal structure of an Ebf1 dimer bound to its palindromic recognition site. The DNA-binding domain adopts a pseudoimmunoglobulin-like fold with novel topology, but is structurally similar to the Rel homology domains of NFAT and NF-kappaB. Ebf1 contacts the DNA with two loop-based modules and a unique Zn coordination motif whereby each Ebf1 monomer interacts with both palindromic half-sites. This unusual mode of DNA recognition generates an extended contact area that may be crucial for the function of Ebf1 in chromatin.
PDB ID: 3MLPDownload
MMDB ID: 86601
PDB Deposition Date: 2010/4/17
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 3MLP: tetrameric; determined by author and by software (PISA)
Molecular Components in 3MLP
Label Count Molecule
Proteins (2 molecules)
Transcription Factor Coe1(Gene symbol: Ebf1)
Molecule annotation
Nucleotide(1 molecule)
DNA (5'- D(*cp*tp*tp*tp*ap*tp*tp*cp*cp*cp*ap*tp*gp*gp*gp*ap*ap*tp*ap*ap*ap*g)- 3')
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB