6K8H

Crystal structure of an omega-transaminase from Sphaerobacter thermophilus

「5D95」から置き換えられました

6K8H の概要

• エントリーDOI: 10.2210/pdb6k8h/pdb
• 分子名称: Aminotransferase class-III, (5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE (3 entities in total)
• 機能のキーワード: transaminase, thermostability, transamination, transferase
• 由来する生物種: Sphaerobacter thermophilus DSM 20745
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 97837.85

構造登録者

Park, H.H.,Kwon, S. (登録日: 2019-06-12, 公開日: 2019-10-09, 最終更新日: 2023-11-22)

主引用文献

Kwon, S.,Lee, J.H.,Kim, C.M.,Ha, H.J.,Lee, S.H.,Lee, C.S.,Jeon, J.H.,So, I.,Park, H.H.
Structural insights into the enzyme specificity of a novel omega-transaminase from the thermophilic bacterium Sphaerobacter thermophilus.
J.Struct.Biol., 208:107395-107395, 2019

PubMed Abstract: Transaminases are pyridoxal 5'-phosphate-dependent enzymes that reversibly catalyze transamination reactions from an amino group donor substrate to an amino group acceptor substrate. ω-Transaminases (ωTAs) utilize compounds with an amino group not at α-carbon position as their amino group donor substrates. Recently, a novel ωTA with broad substrate specificity and high thermostability from the thermophilic bacterium Sphaerobacter thermophilus (St-ωTA) has been reported. Although St-ωTA has been biochemically characterized, little is known about its determinants of substrate specificity. In the present study, we determined the crystal structure of St-ωTA at 1.9 Å resolution to clarify in detail its mechanism of substrate recognition. The structure of St-ωTA revealed that it has a voluminous active site resulting from the unique spatial arrangement of residues comprising its active site. In addition, our molecular docking simulation results suggest that substrate compounds may bind to active site residues via electrostatic interactions or hydrophobic interactions that can be induced by subtle rearrangements of active site residues. On the basis of these structural analyses, we propose a plausible working model of the enzymatic mechanism of St-ωTA. Our results provide profound structural insights into the substrate specificity of St-ωTA and extend the boundaries of knowledge of TAs.

PubMed: 31560999
DOI: 10.1016/j.jsb.2019.09.012

実験手法

X-RAY DIFFRACTION (1.9 Å)