Crystallographic structure of the T domain–DNA complex of the Brachyury transcription factor

Christoph W. Müller () and Bernhard G. Herrmann
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Christoph W. Müller: European Molecular Biology Laboratory, Grenoble Outstation
Bernhard G. Herrmann: Max-Planck-Institut für Immunbiologie

Nature, 1997, vol. 389, issue 6653, 884-888

Abstract: Abstract The mouse Brachyury (T) gene is the prototype of a growing family of so-called T-box genes which encode transcriptional regulators and have been identified in a variety of invertebrates and vertebrates, including humans1,2,3,4,5,6. Mutations in Brachyury and other T-box genes result in drastic embryonic phenotypes, indicating that T-box gene products are essential in tissue specification, morphogenesis and organogenesis7,8,9,10,11. The T-box encodes a DNA-binding domain of about 180 amino-acid residues, the T domain12. Here we report the X-ray structure of the T domain from Xenopus laevis2 in complex with a 24-nucleotide palindromic DNA duplex. We show that the protein is bound as a dimer, interacting with the major and the minor grooves of the DNA. A new type of specific DNA contact is seen, in which a carboxy-terminal helix is deeply embedded into an enlarged minor groove without bending the DNA. Hydrophobic interactions and an unusual main-chain carbonyl contact to a guanine account for sequence-specific recognition in the minor groove by this helix. Thus the structure of this T domain complex with DNA reveals a new way in which a protein can recognize DNA.

Date: 1997
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DOI: 10.1038/39929

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