6XWB

Crystal structure of an R-selective transaminase from Thermomyces stellatus.

6XWB の概要

• エントリーDOI: 10.2210/pdb6xwb/pdb
• 分子名称: R-selective transaminase, 1,2-ETHANEDIOL, PYRIDOXAL-5'-PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: transaminase, transferase
• 由来する生物種: Thermomyces stellatus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82932.28

構造登録者

Gourlay, L.J. (登録日: 2020-01-23, 公開日: 2020-04-15, 最終更新日: 2024-01-24)

主引用文献

Heckmann, C.M.,Gourlay, L.J.,Dominguez, B.,Paradisi, F.
An ( R )-Selective Transaminase From Thermomyces stellatus : Stabilizing the Tetrameric Form.
Front Bioeng Biotechnol, 8:707-707, 2020

PubMed Abstract: The identification and 3D structural characterization of a homolog of the ()-selective transaminase (RTA) from (RTA), from the thermotolerant fungus (RTA) is here reported. The thermostability of RTA (40% retained activity after 7 days at 40°C) was initially attributed to its tetrameric form in solution, however subsequent studies of RTA revealed it also exists predominantly as a tetramer yet, at 40°C, it is inactivated within 48 h. The engineering of a cysteine residue to promote disulfide bond formation across the dimer-dimer interface stabilized both enzymes, with RTA_G205C retaining almost full activity after incubation at 50°C for 7 days. Thus, the role of this mutation was elucidated and the importance of stabilizing the tetramer for overall stability of RTAs is highlighted. RTA accepts the common amine donors ()-methylbenzylamine, isopropylamine, and d-alanine as well as aromatic and aliphatic ketones and aldehydes.

PubMed: 32793563
DOI: 10.3389/fbioe.2020.00707

実験手法

X-RAY DIFFRACTION (2.2 Å)