National Center for
3MLO: Dna Binding Domain Of Early B-cell Factor 1 (ebf1) Bound To Dna (crystal Form I)
Structure of an Ebf1:DNA complex reveals unusual DNA recognition and structural homology with Rel proteins
Genes Dev. (2010) 24 p.2270-2275
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.