5X03

Crystal structure of the C-terminal domain of Bacillus subtilis GabR reveals a closed conformation by the binding of gamma-aminobutyric acid, inducing the transcriptional activation

5X03 の概要

• エントリーDOI: 10.2210/pdb5x03/pdb
• 分子名称: HTH-type transcriptional regulatory protein GabR, PYRIDOXAL-5'-PHOSPHATE, GAMMA-AMINO-BUTANOIC ACID, ... (5 entities in total)
• 機能のキーワード: transcriptional regulator, aminotransferase-like domain, external schiff base, transcription
• 由来する生物種: Bacillus subtilis (strain 168); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84532.66

構造登録者

Park, S.A.,Lee, K.S. (登録日: 2017-01-19, 公開日: 2017-05-24, 最終更新日: 2023-11-15)

主引用文献

Park, S.A.,Park, Y.S.,Lee, K.S.
Crystal structure of the C-terminal domain of Bacillus subtilis GabR reveals a closed conformation by gamma-aminobutyric acid binding, inducing transcriptional activation
Biochem. Biophys. Res. Commun., 487:287-291, 2017

PubMed Abstract: Bacillus subtilis GabR (BsGabR) is involved in the γ-aminobutyric acid (GABA) catabolism as a transcriptional regulator, consisting of an N-terminal helix-turn-helix DNA-binding domain and a C-terminal aminotransferase-like (AT-like) domain. Research on the C-terminal AT-like domain of BsGabR (BsGabR-CTD) has focused on the interaction with GABA as an effector, but most its functional details remain unclear. To understand the underlying mechanism, we report the crystal structure of BsGabR-CTD in complex with pyridoxal 5'-phosphate (PLP) and GABA at 2.0 Å resolution. The structure of ligand-bound BsGabR-CTD revealed two distinct monomeric states in a homodimer. One subunit is a closed-form containing the PLP-GABA adduct, and the other subunit is a PLP-bound open-form. Our structural studies provide a detailed mechanism indicating that the open-to-closed transition by the binding of GABA induces the conformational rearrangement of BsGabR-CTD, which may trigger the activation of transcription.

PubMed: 28412355
DOI: 10.1016/j.bbrc.2017.04.052

実験手法

X-RAY DIFFRACTION (2 Å)