7X4L

Crystal structure of Bacteroides thetaiotaomicron glutamate decarboxylase mutant Y303F-PLP complex

7X4L の概要

• エントリーDOI: 10.2210/pdb7x4l/pdb
• 分子名称: Glutamate decarboxylase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: plp, complex, neutral, biosynthetic protein
• 由来する生物種: Bacteroides thetaiotaomicron VPI-5482
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 330869.92

構造登録者

Liu, S.,Guoming, D.,Yulu, W.,Boting, W.,Xin, F. (登録日: 2022-03-02, 公開日: 2023-05-03, 最終更新日: 2023-11-29)

主引用文献

Liu, S.,Wen, B.,Du, G.,Wang, Y.,Ma, X.,Yu, H.,Zhang, J.,Fan, S.,Zhou, H.,Xin, F.
Coordinated regulation of Bacteroides thetaiotaomicron glutamate decarboxylase activity by multiple elements under different pH.
Food Chem, 403:134436-134436, 2023

PubMed Abstract: Glutamate decarboxylase catalyzes the conversion of glutamate to γ-aminobutyric acid, which plays a vital role in the gut-brain axis. Herein, a novel glutamate decarboxylase from Bacteroides thetaiotaomicron (BTGAD) was heterologously expressed. BTGAD possessed high catalytic efficiency at 60℃ and pH 3.6. As pH response, N-terminal sequence (NTS), C-terminal sequence (CTS), and β-hairpin in BTGAD coordinately regulated its activity under different pH. NTS folded into a loop under acidic pH, and the truncation of NTS severely reduced its activity to 4.2%. While CTS occupied the active site under neutral pH and became disordered to release the inhibition effect under acidic conditions. The β-hairpin, located near the active site, swung and formed open and closed conformations, which acted as an activity switch. This study provides the molecular basis for the coordinated regulation mechanism of BTGAD and lays a theoretical foundation for understanding the metabolism of dietary glutamate and its interaction relationships with the gut-brain axis.

PubMed: 36358099
DOI: 10.1016/j.foodchem.2022.134436

実験手法

X-RAY DIFFRACTION (2.59 Å)