3MLO

DNA binding domain of Early B-cell Factor 1 (Ebf1) bound to DNA (Crystal form I)

Summary for 3MLO

• Entry DOI: 10.2210/pdb3mlo/pdb
• Related: 3MLN 3MLP
• Descriptor: Transcription factor COE1, 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'), ZINC ION, ... (4 entities in total)
• Functional Keywords: transcription factor, pseudo-ig-fold, zn-finger, zn-knuckle, dna, transcription-dna complex, ebf, ebf-1, transcription/dna
• Biological source: Mus musculus (mouse); More
• Cellular location: Nucleus : Q07802
• Total number of polymer chains: 4
• Total formula weight: 64937.89

Authors

Treiber, N.,Treiber, T.,Zocher, G.,Grosschedl, R. (deposition date: 2010-04-17, release date: 2010-12-01, Last modification date: 2024-03-20)

Primary citation

Treiber, N.,Treiber, T.,Zocher, G.,Grosschedl, R.
Structure of an Ebf1:DNA complex reveals unusual DNA recognition and structural homology with Rel proteins
Genes Dev., 24:2270-2275, 2010

PubMed Abstract: 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-κB. 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.

PubMed: 20876732
DOI: 10.1101/gad.1976610

Experimental method

X-RAY DIFFRACTION (3.01 Å)