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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Binding Sites / drug effects
-
Crystallography, X-Ray
-
DNA / chemistry
-
DNA / genetics
-
DNA / metabolism*
-
Electrophoresis, Polyacrylamide Gel
-
Mice
-
Models, Molecular
-
Molecular Sequence Data
-
Mutation
-
Nucleic Acid Conformation
-
Protein Binding
-
Protein Folding
-
Protein Structure, Secondary
-
Protein Structure, Tertiary
-
Proto-Oncogene Proteins c-rel / chemistry
-
Proto-Oncogene Proteins c-rel / genetics
-
Proto-Oncogene Proteins c-rel / metabolism*
-
Trans-Activators / chemistry
-
Trans-Activators / genetics
-
Trans-Activators / metabolism*
-
Zinc / chemistry
-
Zinc / metabolism
Substances
-
Ebf1 protein, mouse
-
Proto-Oncogene Proteins c-rel
-
Trans-Activators
-
DNA
-
Zinc