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Abstract:
Early B-cell factor 1 (Ebf1) is a key transcriptional determinant of B-lymphocyte differentiation whose DNA-binding domainhas no sequence similarity to other transcription factor families. Here we report the crystal structure of an Ebf1 dimer boundto its palindromic recognition site. The DNA-binding domain adopts a pseudoimmunoglobulin-like fold with novel topology, butis structurally similar to the Rel homology domains of NFAT and NF-κB. Ebf1 contacts the DNA with two loop-based modules anda unique Zn coordination motif whereby each Ebf1 monomer interacts with both palindromic half-sites. This unusual mode ofDNA recognition generates an extended contact area that may be crucial for the function of Ebf1 in chromatin.
