6JCB

Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in C2 space group

Summary for 6JCB

• Entry DOI: 10.2210/pdb6jcb/pdb
• Descriptor: CrmG (2 entities in total)
• Functional Keywords: aminotransferase, crmg, transferase
• Biological source: Actinoalloteichus sp. WH1-2216-6
• Total number of polymer chains: 4
• Total formula weight: 228878.08

Authors

Xu, J.,Liu, J. (deposition date: 2019-01-28, release date: 2020-02-05, Last modification date: 2023-11-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.85 Å)