7VP2
Structure of a transcription factor and DNA complex
Summary for 7VP2
| Entry DOI | 10.2210/pdb7vp2/pdb |
| Descriptor | Transcription factor TCP10, DNA (5'-D(*AP*TP*GP*TP*GP*GP*TP*CP*CP*CP*CP*AP*CP*T)-3'), DNA (5'-D(*TP*AP*GP*TP*GP*GP*GP*GP*AP*CP*CP*AP*CP*A)-3'), ... (4 entities in total) |
| Functional Keywords | complex, transcription factor, transcription, transcription-dna complex, dna binding protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
| Total number of polymer chains | 4 |
| Total formula weight | 32334.62 |
| Authors | |
| Primary citation | Zhang, Y.,Xu, Y.P.,Nie, J.K.,Chen, H.,Qin, G.,Wang, B.,Su, X.D. DNA-TCP complex structures reveal a unique recognition mechanism for TCP transcription factor families. Nucleic Acids Res., 51:434-448, 2023 Cited by PubMed Abstract: Plant-specific TCP transcription factors are key regulators of diverse plant functions. TCP transcription factors have long been annotated as basic helix-loop-helix (bHLH) transcription factors according to remote sequence homology without experimental validation, and their consensus DNA-binding sequences and protein-DNA recognition mechanisms have remained elusive. Here, we report the crystal structures of the class I TCP domain from AtTCP15 and the class II TCP domain from AtTCP10 in complex with different double-stranded DNA (dsDNA). The complex structures reveal that the TCP domain is a distinct DNA-binding motif and the homodimeric TCP domains adopt a unique three-site recognition mode, binding to dsDNA mainly through a central pair of β-strands formed by the dimer interface and two basic flexible loops from each monomer. The consensus DNA-binding sequence for class I TCPs is a perfectly palindromic 11 bp (GTGGGNCCCAC), whereas that for class II TCPs is a near-palindromic 11 bp (GTGGTCCCCAC). The unique DNA binding mode allows the TCP domains to display broad specificity for a range of DNA sequences even shorter than 11 bp, adding further complexity to the regulatory network of plant TCP transcription factors. PubMed: 36546761DOI: 10.1093/nar/gkac1171 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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