6SDG
Crystal structure of the DNA binding domain of M. polymorpha Auxin Response Factor 2 (MpARF2) in complex with High Affinity DNA
Summary for 6SDG
Entry DOI | 10.2210/pdb6sdg/pdb |
Descriptor | Auxin response factor, 21-7_A, 21-7_B (3 entities in total) |
Functional Keywords | transcription factor, dna binding, nucleus, hormone response, transcription |
Biological source | Marchantia polymorpha (Liverwort) More |
Total number of polymer chains | 4 |
Total formula weight | 94276.57 |
Authors | Crespo, I.,Weijers, D.,Boer, D.R. (deposition date: 2019-07-27, release date: 2020-04-08, Last modification date: 2024-01-24) |
Primary citation | Kato, H.,Mutte, S.K.,Suzuki, H.,Crespo, I.,Das, S.,Radoeva, T.,Fontana, M.,Yoshitake, Y.,Hainiwa, E.,van den Berg, W.,Lindhoud, S.,Ishizaki, K.,Hohlbein, J.,Borst, J.W.,Boer, D.R.,Nishihama, R.,Kohchi, T.,Weijers, D. Design principles of a minimal auxin response system. Nat.Plants, 6:473-482, 2020 Cited by PubMed Abstract: Auxin controls numerous growth processes in land plants through a gene expression system that modulates ARF transcription factor activity. Gene duplications in families encoding auxin response components have generated tremendous complexity in most land plants, and neofunctionalization enabled various unique response outputs during development. However, it is unclear what fundamental biochemical principles underlie this complex response system. By studying the minimal system in Marchantia polymorpha, we derive an intuitive and simple model where a single auxin-dependent A-ARF activates gene expression. It is antagonized by an auxin-independent B-ARF that represses common target genes. The expression patterns of both ARF proteins define developmental zones where auxin response is permitted, quantitatively tuned or prevented. This fundamental design probably represents the ancestral system and formed the basis for inflated, complex systems. PubMed: 32415296DOI: 10.1038/s41477-020-0662-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.96 Å) |
Structure validation
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