4ZDS
Crystal Structure of core DNA binding domain of Arabidopsis Thaliana Transcription Factor Ethylene-Insensitive 3
Summary for 4ZDS
Entry DOI | 10.2210/pdb4zds/pdb |
Descriptor | Protein ETHYLENE INSENSITIVE 3 (2 entities in total) |
Functional Keywords | dna binding domain transcription factor, transcription activator |
Biological source | Arabidopsis thaliana (Mouse-ear cress) |
Cellular location | Nucleus: O24606 |
Total number of polymer chains | 2 |
Total formula weight | 30701.56 |
Authors | |
Primary citation | Song, J.,Zhu, C.,Zhang, X.,Wen, X.,Liu, L.,Peng, J.,Guo, H.,Yi, C. Biochemical and Structural Insights into the Mechanism of DNA Recognition by Arabidopsis ETHYLENE INSENSITIVE3. Plos One, 10:e0137439-e0137439, 2015 Cited by PubMed Abstract: Gaseous hormone ethylene regulates numerous stress responses and developmental adaptations in plants by controlling gene expression via transcription factors ETHYLENE INSENSITIVE3 (EIN3) and EIN3-Like1 (EIL1). However, our knowledge regarding to the accurate definition of DNA-binding domains (DBDs) within EIN3 and also the mechanism of specific DNA recognition by EIN3 is limited. Here, we identify EIN3 82-352 and 174-306 as the optimal and core DBDs, respectively. Results from systematic biochemical analyses reveal that both the number of EIN3-binding sites (EBSs) and the spacing length between two EBSs affect the binding affinity of EIN3; accordingly, a new DNA probe which has higher affinity with EIN3 than ERF1 is also designed. Furthermore, we show that palindromic repeat sequences in ERF1 promoter are not necessary for EIN3 binding. Finally, we provide, to our knowledge, the first crystal structure of EIN3 core DBD, which contains amino acid residues essential for DNA binding and signaling. Collectively, these data suggest the detailed mechanism of DNA recognition by EIN3 and provide an in-depth view at molecular level for the transcriptional regulation mediated by EIN3. PubMed: 26352699DOI: 10.1371/journal.pone.0137439 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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