7ACM

Crystal structure of E. coli HTH-type transcriptional regulator RcdA in complex with TMAO at 1.76 A resolution

7ACM の概要

• エントリーDOI: 10.2210/pdb7acm/pdb
• 分子名称: HTH-type transcriptional regulator RcdA, trimethylamine oxide (3 entities in total)
• 機能のキーワード: transcription factor, hth motif, dna-binding protein, gene regulation
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40808.92

構造登録者

Pietrzyk-Brzezinska, A.J.,Cociurovscaia, A. (登録日: 2020-09-11, 公開日: 2021-08-18, 最終更新日: 2024-01-31)

主引用文献

Pietrzyk-Brzezinska, A.J.,Cociurovscaia, A.
Structures of the TetR-like transcription regulator RcdA alone and in complexes with ligands.
Proteins, 90:33-44, 2022

PubMed Abstract: RcdA is a helix-turn-helix (HTH) transcriptional regulator belonging to the TetR family. The protein regulates the transcription of curlin subunit gene D, the master regulator of biofilm formation. Moreover, it was predicted that it might be involved in the regulation of up to 27 different genes. However, an effector of RcdA and the environmental conditions which trigger RcdA action remain unknown. Herein, we report the first crystal structures of RcdA in complexes with ligands, trimethylamine N-oxide (TMAO) and tris(hydroxymethyl)aminomethane (Tris), which might serve as RcdA effectors. Based on these structures, the ligand-binding pocket of RcdA was characterized in detail. The conservation of the amino acid residues forming the ligand-binding cavity was analyzed and the comprehensive search for RcdA structural homologs was performed. This analysis indicated that RcdA is structurally similar to multidrug-binding TetR family members, however, its ligand-binding cavity differs significantly from the pockets of its structural homologs. The interaction of RcdA with TMAO and Tris indicates that the protein might be involved in alkaline stress response.

PubMed: 34288132
DOI: 10.1002/prot.26183

実験手法

X-RAY DIFFRACTION (1.763 Å)