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1UT4

Structure of the conserved domain of ANAC, a member of the NAC family of transcription factors

1UT4 の概要
エントリーDOI10.2210/pdb1ut4/pdb
関連するPDBエントリー1UT7
分子名称NO APICAL MERISTEM PROTEIN (2 entities in total)
機能のキーワードtranscription regulation, transcription, transcription factor, dna binding, abscisic acid response, arabidopsis thaliana, nac domain
由来する生物種ARABIDOPSIS THALIANA (MOUSE-EAR CRESS)
細胞内の位置Nucleus : Q9C932
タンパク質・核酸の鎖数2
化学式量合計39561.33
構造登録者
Ernst, H.A.,Olsen, A.N.,Skriver, K.,Larsen, S.,Lo Leggio, L. (登録日: 2003-12-03, 公開日: 2004-03-19, 最終更新日: 2024-05-08)
主引用文献Ernst, H.A.,Olsen, A.N.,Skriver, K.,Larsen, S.,Lo Leggio, L.
Structure of the Conserved Domain of Anac, a Member of the Nac Family of Transcription Factors
Embo Rep., 5:297-, 2004
Cited by
PubMed Abstract: The structure of the DNA-binding NAC domain of Arabidopsis ANAC (abscisic-acid-responsive NAC) has been determined by X-ray crystallography to 1.9A resolution (Protein Data Bank codes 1UT4 and 1UT7). This is the first structure determined for a member of the NAC family of plant-specific transcriptional regulators. NAC proteins are characterized by their conserved N-terminal NAC domains that can bind both DNA and other proteins. NAC proteins are involved in developmental processes, including formation of the shoot apical meristem, floral organs and lateral shoots, as well as in plant hormonal control and defence. The NAC domain does not possess a classical helix-turn-helix motif; instead it reveals a new transcription factor fold consisting of a twisted beta-sheet surrounded by a few helical elements. The functional dimer formed by the NAC domain was identified in the structure, which will serve as a structural template for understanding NAC protein function at the molecular level.
PubMed: 15083810
DOI: 10.1038/SJ.EMBOR.7400093
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 1ut4
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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