5YSH

Diol dehydratase - alpha/T172A mutant complexed with AdoCbl, aerobically-prepared crystal

5YSH の概要

• エントリーDOI: 10.2210/pdb5ysh/pdb
• 分子名称: Diol dehydrase alpha subunit, Diol dehydrase beta subunit, Diol dehydrase gamma subunit, ... (9 entities in total)
• 機能のキーワード: adenosylcobalamin, radical enzyme, lyase
• 由来する生物種: Klebsiella oxytoca; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 397950.76

構造登録者

Shibata, N. (登録日: 2017-11-14, 公開日: 2018-09-19, 最終更新日: 2023-11-22)

主引用文献

Shibata, N.,Sueyoshi, Y.,Higuchi, Y.,Toraya, T.
Direct Participation of a Peripheral Side Chain of a Corrin Ring in Coenzyme B12Catalysis.
Angew. Chem. Int. Ed. Engl., 57:7830-7835, 2018

PubMed Abstract: The crystal structures of the B -dependent isomerases (eliminating) diol dehydratase and ethanolamine ammonia-lyase complexed with adenosylcobalamin were solved with and without substrates. The structures revealed that the peripheral a-acetamide side chain of the corrin ring directly interacts with the adenosyl group to maintain the group in the catalytic position, and that this side chain swings between the original and catalytic positions in a synchronized manner with the radical shuttling between the coenzyme and substrate/product. Mutations involving key residues that cooperatively participate in the positioning of the adenosyl group, directly or indirectly through the interaction with the a-side chain, decreased the turnover rate and increased the relative rate of irreversible inactivation caused by undesirable side reactions. These findings guide the engineering of enzymes for improved catalysis and producing useful chemicals by utilizing the high reactivity of radical species.

PubMed: 29797764
DOI: 10.1002/anie.201803591

実験手法

X-RAY DIFFRACTION (1.9 Å)