8HT2

Crystal structure of Acetylornithine aminotransferase from Corynebacterium glutamicum

Summary for 8HT2

• Entry DOI: 10.2210/pdb8ht2/pdb
• Descriptor: Acetylornithine aminotransferase (2 entities in total)
• Functional Keywords: acetylornithine aminotransferase; corynebacterium glutamicum, transferase
• Biological source: Corynebacterium glutamicum ATCC 13032
• Total number of polymer chains: 2
• Total formula weight: 84636.40

Authors

Ki, D.,Kim, K.-J. (deposition date: 2022-12-20, release date: 2024-01-17, Last modification date: 2024-06-05)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.65 Å)