8GYZ

Crystal structure of transcription factor TGA7 from Arabidopsis

Summary for 8GYZ

• Entry DOI: 10.2210/pdb8gyz/pdb
• Descriptor: Transcription factor TGA7, PALMITIC ACID (3 entities in total)
• Functional Keywords: tga7-palmitate complex, transcription factor, dna binding protein
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 2
• Total formula weight: 70031.13

Authors

Shi, X.Q.,Che, Z.,Ming, Z.H. (deposition date: 2022-09-24, release date: 2022-11-30, Last modification date: 2024-05-01)

Primary citation

Shi, X.,Che, Z.,Xu, G.,Ming, Z.
Crystal structure of transcription factor TGA7 from Arabidopsis.
Biochem.Biophys.Res.Commun., 637:322-330, 2022

PubMed Abstract: TGA family of transcription factors play important roles in the systemic acquired resistance (SAR) in plants. In SAR, TGA7 binds to the activation sequence-1 (as-1) in the promoter region of SAR related genes and regulates their expressions in an NPR1 dependent manner. Despite its important roles in plant immunity, the molecular mechanism for DNA binding of TGA7 remains unclear. In the present work, we resolved the crystal structure of TGA7 dimers at a resolution of 2.06 Å, in which each monomer binds one molecule of palmitate. Further biochemical studies revealed that TGA7 specifically binds to the TGACG boxes of as-1 DNA in the form of homodimers, and it has specific requirements for the relative spacing and orientation of the two TGACG boxes. Moreover, we built a TGA7-DNA complex model and confirmed by site-directed mutagenesis that amino acid residue R109 in the DNA binding domain (DBD) of TGA7 is a key residue responsible for DNA recognition. Our work offers a good example for structural and functional studies of TGA proteins, and provides key clues to understand the DNA binding mechanism of TGA proteins in the SAR.

PubMed: 36423378
DOI: 10.1016/j.bbrc.2022.11.039

Experimental method

X-RAY DIFFRACTION (2.06 Å)