5C7E

Crystal structure of the rice Topless related protein 2 (TPR2) N-terminal domain (1-209) in complex with Arabidopsis IAA10 peptide

5C7E の概要

• エントリーDOI: 10.2210/pdb5c7e/pdb
• 関連するPDBエントリー: 4ZHE 5C6Q 5C6V 5C7F
• 分子名称: ASPR2 protein, Auxin-responsive protein IAA10, ZINC ION, ... (4 entities in total)
• 機能のキーワード: transcriptional corepressor, alpha-helical structure, tetrameric protein, plant transcriptional repression, transcription, plant development
• 由来する生物種: Oryza sativa (Rice); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 156775.76

構造登録者

Ke, J.,Ma, H.,Gu, X.,Brunzelle, J.S.,Xu, H.E.,Melcher, K. (登録日: 2015-06-24, 公開日: 2015-08-05, 最終更新日: 2023-09-27)

主引用文献

Ke, J.,Ma, H.,Gu, X.,Thelen, A.,Brunzelle, J.S.,Li, J.,Xu, H.E.,Melcher, K.
Structural basis for recognition of diverse transcriptional repressors by the TOPLESS family of corepressors.
Sci Adv, 1:e1500107-e1500107, 2015

PubMed Abstract: TOPLESS (TPL) and TOPLESS-related (TPR) proteins comprise a conserved family of plant transcriptional corepressors that are related to Tup1, Groucho, and TLE (transducin-like enhancer of split) corepressors in yeast, insects, and mammals. In plants, TPL/TPR corepressors regulate development, stress responses, and hormone signaling through interaction with small ethylene response factor-associated amphiphilic repression (EAR) motifs found in diverse transcriptional repressors. How EAR motifs can interact with TPL/TPR proteins is unknown. We confirm the amino-terminal domain of the TPL family of corepressors, which we term TOPLESS domain (TPD), as the EAR motif-binding domain. To understand the structural basis of this interaction, we determined the crystal structures of the TPD of rice (Os) TPR2 in apo (apo protein) state and in complexes with the EAR motifs from Arabidopsis NINJA (novel interactor of JAZ), IAA1 (auxin-responsive protein 1), and IAA10, key transcriptional repressors involved in jasmonate and auxin signaling. The OsTPR2 TPD adopts a new fold of nine helices, followed by a zinc finger, which are arranged into a disc-like tetramer. The EAR motifs in the three different complexes adopt a similar extended conformation with the hydrophobic residues fitting into the same surface groove of each OsTPR2 monomer. Sequence alignments and structure-based mutagenesis indicate that this mode of corepressor binding is highly conserved in a large set of transcriptional repressors, thus providing a general mechanism for gene repression mediated by the TPL family of corepressors.

PubMed: 26601214
DOI: 10.1126/sciadv.1500107

実験手法

X-RAY DIFFRACTION (3.1 Å)