4LDX
Crystal structure of the DNA binding domain of arabidopsis thaliana auxin response factor 1 (ARF1) in complex with protomor-like sequence ER7
4LDX の概要
| エントリーDOI | 10.2210/pdb4ldx/pdb |
| 関連するPDBエントリー | 4LDU 4LDv 4LDw 4LDy |
| 分子名称 | Auxin response factor 1, ER7, forward sequence, ER7, reverse sequence, ... (4 entities in total) |
| 機能のキーワード | protein-dna complex, transcription factor, promotor dna, nucleus, transcription-dna complex, transcription/dna |
| 由来する生物種 | Arabidopsis thaliana (mouse-ear cress,thale-cress) 詳細 |
| 細胞内の位置 | Nucleus: Q8L7G0 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 95250.37 |
| 構造登録者 | Boer, D.R.,Freire-Rios, A.,van den Berg, W.M.A.,Weijers, D.,Coll, M. (登録日: 2013-06-25, 公開日: 2014-02-12, 最終更新日: 2023-09-20) |
| 主引用文献 | Boer, D.R.,Freire-Rios, A.,van den Berg, W.A.,Saaki, T.,Manfield, I.W.,Kepinski, S.,Lopez-Vidrieo, I.,Franco-Zorrilla, J.M.,de Vries, S.C.,Solano, R.,Weijers, D.,Coll, M. Structural Basis for DNA Binding Specificity by the Auxin-Dependent ARF Transcription Factors. Cell(Cambridge,Mass.), 156:577-589, 2014 Cited by PubMed Abstract: Auxin regulates numerous plant developmental processes by controlling gene expression via a family of functionally distinct DNA-binding auxin response factors (ARFs), yet the mechanistic basis for generating specificity in auxin response is unknown. Here, we address this question by solving high-resolution crystal structures of the pivotal Arabidopsis developmental regulator ARF5/MONOPTEROS (MP), its divergent paralog ARF1, and a complex of ARF1 and a generic auxin response DNA element (AuxRE). We show that ARF DNA-binding domains also homodimerize to generate cooperative DNA binding, which is critical for in vivo ARF5/MP function. Strikingly, DNA-contacting residues are conserved between ARFs, and we discover that monomers have the same intrinsic specificity. ARF1 and ARF5 homodimers, however, differ in spacing tolerated between binding sites. Our data identify the DNA-binding domain as an ARF dimerization domain, suggest that ARF dimers bind complex sites as molecular calipers with ARF-specific spacing preference, and provide an atomic-scale mechanistic model for specificity in auxin response. PubMed: 24485461DOI: 10.1016/j.cell.2013.12.027 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.9 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






