7XJT

Catabolic ornithine carbamoyltransferases (OTCs) from Psychrobacter sp. PAMC 21119

7XJT の概要

• エントリーDOI: 10.2210/pdb7xjt/pdb
• 関連するPDBエントリー: 7X99
• 分子名称: Ornithine carbamoyltransferases, SULFATE ION (3 entities in total)
• 機能のキーワード: ornithine carbamoyltransferases, catabolic otc, transferase
• 由来する生物種: Psychrobacter sp. PAMC 21119
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 152449.06

構造登録者

Do, H.,Lee, J.H. (登録日: 2022-04-18, 公開日: 2022-08-31, 最終更新日: 2024-04-03)

主引用文献

Do, H.,Nguyen, D.L.,Lee, C.W.,Lee, M.J.,Oh, H.,Hwang, J.,Han, S.J.,Lee, S.G.,Lee, J.H.
Comparative structural insight into the unidirectional catalysis of ornithine carbamoyltransferases from Psychrobacter sp. PAMC 21119.
Plos One, 17:e0274019-e0274019, 2022

PubMed Abstract: Ornithine carbamoyltransferases (OTCs) are involved in the arginine deiminase (ADI) pathway and in arginine biosynthesis. Two OTCs in a pair are named catalytic OTC (cOTC) and anabolic OTC (aOTC). The cOTC is responsible for catalyzing the third step of the ADI pathway to catabolize citrulline into carbamoyl phosphate (CP), as well as ornithine, and displays CP cooperativity. In contrast, aOTC catalyzes the biosynthesis of citrulline from CP and ornithine in vivo and is thus involved in arginine biosynthesis. Structural and biochemical analyses were employed to investigate the CP cooperativity and unidirectional function of two sequentially similar OTCs (32.4% identity) named Ps_cOTC and Ps_aOTC from Psychrobacter sp. PAMC 21119. Comparison of the trimeric structure of these two OTCs indicated that the 80s loop of Ps_cOTC has a unique conformation that may influence cooperativity by connecting the CP binding site and the center of the trimer. The corresponding 80s loop region of in Ps_aOTC was neither close to the CP binding site nor connected to the trimer center. In addition, results from the thermal shift assay indicate that each OTC prefers the substrate for the unidirectional process. The active site exhibited a blocked binding site for CP in the Ps_cOTC structure, whereas residues at the active site in Ps_aOTC established a binding site to facilitate CP binding. Our data provide novel insights into the unidirectional catalysis of OTCs and cooperativity, which are distinguishable features of two metabolically specialized proteins.

PubMed: 36149917
DOI: 10.1371/journal.pone.0274019

実験手法

X-RAY DIFFRACTION (2.598 Å)