1XBR

T DOMAIN FROM XENOPUS LAEVIS BOUND TO DNA

Summary for 1XBR

• Entry DOI: 10.2210/pdb1xbr/pdb
• Descriptor: DNA (5'-D(*AP*AP*TP*TP*TP*CP*AP*CP*AP*CP*CP*TP*AP*GP*GP*TP*G P*TP*GP*AP*AP*AP* TP*T)-3'), PROTEIN (T PROTEIN) (3 entities in total)
• Functional Keywords: complex (transcription factor-dna), transcription factor, dna-binding protein, transcription-dna complex, transcription/dna
• Cellular location: Nucleus: P24781
• Total number of polymer chains: 4
• Total formula weight: 56884.12

Authors

Muller, C.W. (deposition date: 1997-07-16, release date: 1998-01-16, Last modification date: 2024-02-14)

Primary citation

Muller, C.W.,Herrmann, B.G.
Crystallographic structure of the T domain-DNA complex of the Brachyury transcription factor.
Nature, 389:884-888, 1997

PubMed 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 humans. 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 organogenesis. The T-box encodes a DNA-binding domain of about 180 amino-acid residues, the T domain. Here we report the X-ray structure of the T domain from Xenopus laevis 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.

PubMed: 9349824
DOI: 10.1038/39929

Experimental method

X-RAY DIFFRACTION (2.5 Å)