5ZD4

Crystal structure of MBP-fused BIL1/BZR1 in complex with double-stranded DNA

5ZD4 の概要

• エントリーDOI: 10.2210/pdb5zd4/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose-binding periplasmic protein,Protein BRASSINAZOLE-RESISTANT 1, DNA (5'-D(*TP*TP*CP*AP*CP*AP*CP*GP*TP*GP*TP*GP*AP*AP*A)-3'), alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: transcription factor, brassinosteroid, plant, transcription
• 由来する生物種: Escherichia coli O157:H7; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 219453.49

構造登録者

Nosaki, S.,Miyakawa, T.,Xu, Y.,Nakamura, A.,Hirabayashi, K.,Tanokura, M. (登録日: 2018-02-22, 公開日: 2018-08-29, 最終更新日: 2023-11-22)

主引用文献

Nosaki, S.,Miyakawa, T.,Xu, Y.,Nakamura, A.,Hirabayashi, K.,Asami, T.,Nakano, T.,Tanokura, M.
Structural basis for brassinosteroid response by BIL1/BZR1.
Nat Plants, 4:771-776, 2018

PubMed Abstract: BRZ-INSENSITIVE-LONG HYPOCOTYL 1 (BIL1)/BRASSINAZOLE-RESISTANT 1 (BZR1) is a master transcription factor of brassinosteroid (BR) signalling. The varieties of nucleobase recognition of the NN-BRRE-core motif (NNCGTG), one of variant G-box motifs, distinguish BIL1/BZR1 from basic helix-loop-helix transcription factors, underlying the specific regulation of BR-responsive genes. Here, we show the non-canonical bHLH dimer formation of BIL1/BZR1 to optimize the interaction network with DNA and the orientation of a key residue for NN-BRRE-core motif recognition.

PubMed: 30287951
DOI: 10.1038/s41477-018-0255-1

実験手法

X-RAY DIFFRACTION (2.17 Å)