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3DFV

Adjacent GATA DNA binding

Summary for 3DFV
Entry DOI10.2210/pdb3dfv/pdb
Related3DFX
DescriptorDNA (5'-D(*DTP*DTP*DCP*DTP*DGP*DAP*DTP*DAP*DAP*DGP*DAP*DCP*DTP*DTP*DAP*DTP*DCP*DTP*DGP*DC)-3'), DNA (5'-D(*DAP*DAP*DGP*DCP*DAP*DGP*DAP*DTP*DAP*DAP*DGP*DTP*DCP*DTP*DTP*DAP*DTP*DCP*DAP*DG)-3'), Trans-acting T-cell-specific transcription factor GATA-3, ... (4 entities in total)
Functional Keywordstranscription/dna, activator, dna-binding, metal-binding, nucleus, transcription, transcription regulation, zinc, zinc-finger, transcription-dna complex
Biological sourceMus musculus (mouse)
Cellular locationNucleus: P23772
Total number of polymer chains4
Total formula weight26483.93
Authors
Bates, D.L.,Kim, G.K.,Guo, L.,Chen, L. (deposition date: 2008-06-12, release date: 2008-07-29, Last modification date: 2024-10-30)
Primary citationBates, D.L.,Chen, Y.,Kim, G.,Guo, L.,Chen, L.
Crystal structures of multiple GATA zinc fingers bound to DNA reveal new insights into DNA recognition and self-association by GATA.
J.Mol.Biol., 381:1292-1306, 2008
Cited by
PubMed Abstract: The GATA family of transcription factors (GATA1-6) binds selected GATA sites in vertebrate genomes to regulate specific gene expression. Although vertebrate GATA factors have two highly conserved zinc finger motifs, how the two fingers act together to recognize functional DNA elements is not well understood. Here we determined the crystal structures of the C-terminal zinc finger of mouse GATA3 bound to DNA containing two variously arranged GATA binding sites. Our structures and accompanying biochemical analyses reveal two distinct modes of DNA binding by GATA to closely arranged sites. One mode involves cooperative binding by two GATA factors that interact with each other through protein-protein interactions. The other involves simultaneous binding of the N-terminal zinc finger (N-finger) and the C-terminal zinc finger of the same GATA factor. Our studies represent the first crystallographic analysis of GATA zinc fingers bound to DNA and provide new insights into the DNA recognition mechanism by the GATA zinc finger. Our crystal structure also reveals a dimerization interface in GATA that has previously been shown to be important for GATA self-association. These findings significantly advance our understanding of the structure and function of GATA and provide an important framework for further investigating the in vivo mechanisms of GATA-dependent gene regulation.
PubMed: 18621058
DOI: 10.1016/j.jmb.2008.06.072
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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