6JIX

The cyrstal structure of taurine:2-oxoglutarate aminotransferase from Bifidobacterium kashiwanohense, in complex with PLP and glutamate

6JIX の概要

• エントリーDOI: 10.2210/pdb6jix/pdb
• 分子名称: taurine:2-oxoglutarate aminotransferase, GLUTAMIC ACID, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: aminotransferase, pyridoxal 5' phosphate, glutamate, 2-oxoglutarate, transferase
• 由来する生物種: Bifidobacterium kashiwanohense PV20-2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 201548.63

構造登録者

Li, M.,Lin, L.,Zhang, Y.,Yuchi, Z. (登録日: 2019-02-23, 公開日: 2020-01-01, 最終更新日: 2023-11-29)

主引用文献

Li, M.,Wei, Y.,Yin, J.,Lin, L.,Zhou, Y.,Hua, G.,Cao, P.,Ang, E.L.,Zhao, H.,Yuchi, Z.,Zhang, Y.
Biochemical and structural investigation of taurine:2-oxoglutarate aminotransferase fromBifidobacterium kashiwanohense.
Biochem.J., 476:1605-1619, 2019

PubMed Abstract: Taurine aminotransferases catalyze the first step in taurine catabolism in many taurine-degrading bacteria and play an important role in bacterial taurine metabolism in the mammalian gut. Here, we report the biochemical and structural characterization of a new taurine:2-oxoglutarate aminotransferase from the human gut bacterium (Toa). Biochemical assays revealed high specificity of Toa for 2-oxoglutarate as the amine acceptor. The crystal structure of Toa in complex with pyridoxal 5'-phosphate (PLP) and glutamate was determined at 2.7 Å resolution. The enzyme forms a homodimer, with each monomer exhibiting a typical type I PLP-enzyme fold and conserved PLP-coordinating residues interacting with the PLP molecule. Two glutamate molecules are bound in sites near the predicted active site and they may occupy a path for substrate entry and product release. Molecular docking reveals a role for active site residues Trp21 and Arg156, conserved in Toa enzymes studied to date, in interacting with the sulfonate group of taurine. Bioinformatics analysis shows that the close homologs of Toa are also present in other anaerobic gut bacteria.

PubMed: 31088892
DOI: 10.1042/BCJ20190206

実験手法

X-RAY DIFFRACTION (2.647 Å)