A putative DNA-binding domain with a conserved structure is found in several different protein families. The core structure of the domain consists of a three-helical fold that is architecturally similar to that of the "winged-helix" fold, but is topologically distinct. Representatives of this domain can be found in domains B1 and B5 from the beta subunit of phenylalanine-tRNA synthetases [1], the C-terminal region of the DNA/RPA-binding domain of the DNA excision repair factor XPA [2], the N-terminal domain of the transcriptional activators BmrR and MtaN [3], the most conserved domain of the retinal development protein Dachshund [4], and the DNA-binding domain of the gpNU1 subunit from the bacteriophage lambda viral packing protein terminase [5].

1. Structure at 2.6 A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese. Acta Crystallogr. D Biol. Crystallogr. 57, 1534-44
2. Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies. Biochemistry 38, 15116-28
3. Crystal structure of the transcription activator BmrR bound to DNA and a drug. Nature 409, 378-82
4. Structure of the retinal determination protein Dachshund reveals a DNA binding motif. Structure 10, 787-95
5. Insights into specific DNA recognition during the assembly of a viral genome packaging machine. Mol. Cell 9, 981-91

A putative DNA-binding domain with a conserved structure is found in several different protein fa
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