8HT2

Crystal structure of Acetylornithine aminotransferase from Corynebacterium glutamicum

8HT2 の概要

• エントリーDOI: 10.2210/pdb8ht2/pdb
• 分子名称: Acetylornithine aminotransferase (2 entities in total)
• 機能のキーワード: acetylornithine aminotransferase; corynebacterium glutamicum, transferase
• 由来する生物種: Corynebacterium glutamicum ATCC 13032
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84636.40

構造登録者

Ki, D.,Kim, K.-J. (登録日: 2022-12-20, 公開日: 2024-01-17, 最終更新日: 2024-06-05)

主引用文献

Ki, D.,Hong, H.,Kim, I.K.,Kim, K.J.
Crystal Structure and Functional Characterization of Acetylornithine Aminotransferase from Corynebacterium glutamicum.
J.Agric.Food Chem., 71:8471-8478, 2023

PubMed Abstract: The amino acids l-arginine and l-ornithine are widely used in animal feed and as health supplements and pharmaceutical compounds. In arginine biosynthesis, acetylornithine aminotransferase (AcOAT) uses pyridoxal-5'-phosphate (PLP) as a cofactor for amino group transfer. Here, we determined the crystal structures of the apo and PLP complex forms of AcOAT from (AcOAT). Our structural observations revealed that AcOAT undergoes an order-to-disorder conformational change upon binding with PLP. Additionally, we observed that unlike other AcOATs, AcOAT exists as a tetramer. Subsequently, we identified the key residues involved in PLP and substrate binding based on structural analysis and site-directed mutagenesis. This study might provide structural insights on AcOAT, which can be utilized for the development of improved l-arginine production enzymes.

PubMed: 37230944
DOI: 10.1021/acs.jafc.3c00659

実験手法

X-RAY DIFFRACTION (2.65 Å)