3SWM
The NAC domain of ANAC019 in complex with DNA, gold derivative
Summary for 3SWM
| Entry DOI | 10.2210/pdb3swm/pdb |
| Related | 3SWP 4DUL |
| Descriptor | NAC domain-containing protein 19, oligonucleotide forward, oligonucleotide reverse, ... (4 entities in total) |
| Functional Keywords | mostly beta-sheet, transcription factor, transcription-dna complex, transcription/dna |
| Biological source | Arabidopsis thaliana (mouse-ear cress) |
| Cellular location | Nucleus: Q9C932 |
| Total number of polymer chains | 6 |
| Total formula weight | 99058.09 |
| Authors | Welner, D.,Lo Leggio, L. (deposition date: 2011-07-14, release date: 2012-04-11, Last modification date: 2023-09-13) |
| Primary citation | Welner, D.H.,Lindemose, S.,Grossmann, J.G.,Mollegaard, N.E.,Olsen, A.N.,Helgstrand, C.,Skriver, K.,Lo Leggio, L. DNA binding by the plant-specific NAC transcription factors in crystal and solution: a firm link to WRKY and GCM transcription factors. Biochem.J., 444:395-404, 2012 Cited by PubMed Abstract: NAC (NAM/ATAF/CUC) plant transcription factors regulate essential processes in development, stress responses and nutrient distribution in important crop and model plants (rice, Populus, Arabidopsis), which makes them highly relevant in the context of crop optimization and bioenergy production. The structure of the DNA-binding NAC domain of ANAC019 has previously been determined by X-ray crystallography, revealing a dimeric and predominantly β-fold structure, but the mode of binding to cognate DNA has remained elusive. In the present study, information from low resolution X-ray structures and small angle X-ray scattering on complexes with oligonucleotides, mutagenesis and (DNase I and uranyl photo-) footprinting, is combined to form a structural view of DNA-binding, and for the first time provide experimental evidence for the speculated relationship between plant-specific NAC proteins, WRKY transcription factors and the mammalian GCM (Glial cell missing) transcription factors, which all use a β-strand motif for DNA-binding. The structure shows that the NAC domain inserts the edge of its core β-sheet into the major groove, while leaving the DNA largely undistorted. The structure of the NAC-DNA complex and a new crystal form of the unbound NAC also indicate limited flexibility of the NAC dimer arrangement, which could be important in recognizing suboptimal binding sites. PubMed: 22455904DOI: 10.1042/BJ20111742 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.25 Å) |
Structure validation
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