6JCA

Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in I222 space group

6JCA の概要

• エントリーDOI: 10.2210/pdb6jca/pdb
• 分子名称: CrmG, GLYCEROL, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: aminotransferase, crmg, transferase
• 由来する生物種: Actinoalloteichus sp. WH1-2216-6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 114957.17

構造登録者

Xu, J.,Liu, J. (登録日: 2019-01-28, 公開日: 2020-02-05, 最終更新日: 2023-11-22)

主引用文献

Xu, J.,Tang, X.,Zhu, Y.,Yu, Z.,Su, K.,Zhang, Y.,Dong, Y.,Zhu, W.,Zhang, C.,Wu, R.,Liu, J.
Structural studies reveal flexible roof of active site responsible for omega-transaminase CrmG overcoming by-product inhibition.
Commun Biol, 3:455-455, 2020

PubMed Abstract: Amine compounds biosynthesis using ω-transaminases has received considerable attention in the pharmaceutical industry. However, the application of ω-transaminases was hampered by the fundamental challenge of severe by-product inhibition. Here, we report that ω-transaminase CrmG from Actinoalloteichus cyanogriseus WH1-2216-6 is insensitive to inhibition from by-product α-ketoglutarate or pyruvate. Combined with structural and QM/MM studies, we establish the detailed catalytic mechanism for CrmG. Our structural and biochemical studies reveal that the roof of the active site in PMP-bound CrmG is flexible, which will facilitate the PMP or by-product to dissociate from PMP-bound CrmG. Our results also show that amino acceptor caerulomycin M (CRM M), but not α-ketoglutarate or pyruvate, can form strong interactions with the roof of the active site in PMP-bound CrmG. Based on our results, we propose that the flexible roof of the active site in PMP-bound CrmG may facilitate CrmG to overcome inhibition from the by-product.

PubMed: 32814814
DOI: 10.1038/s42003-020-01184-w

実験手法

X-RAY DIFFRACTION (2.1 Å)