5C6V

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

Summary for 5C6V

• Entry DOI: 10.2210/pdb5c6v/pdb
• Related: 4ZHE 5C6Q 5C7E 5C7F
• Descriptor: ASPR2 protein, AFP homolog 2 (3 entities in total)
• Functional Keywords: transcriptional corepressor, alpha-helical structure, tetrameric protein, plant transcriptional repression, transcription, plant development
• Biological source: Oryza sativa (Rice); More
• Total number of polymer chains: 8
• Total formula weight: 104083.28

Authors

Ke, J.,Ma, H.,Gu, X.,Brunzelle, J.S.,Xu, H.E.,Melcher, K. (deposition date: 2015-06-23, release date: 2015-08-05, Last modification date: 2023-09-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.1 Å)