6LIU

Crystal structure of apo Tyrosine decarboxylase

6LIU の概要

• エントリーDOI: 10.2210/pdb6liu/pdb
• 分子名称: Tyrosine/DOPA decarboxylase 2 (2 entities in total)
• 機能のキーワード: apo form, decarboxylase, plp binding, tyrosine, lyase
• 由来する生物種: Papaver somniferum (Opium poppy)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 356541.61

構造登録者

Yu, J.,Wang, H.,Yao, M. (登録日: 2019-12-13, 公開日: 2020-02-12, 最終更新日: 2024-05-01)

主引用文献

Wang, H.,Yu, J.,Satoh, Y.,Nakagawa, Y.,Tanaka, R.,Kato, K.,Yao, M.
Crystal structures clarify cofactor binding of plant tyrosine decarboxylase.
Biochem.Biophys.Res.Commun., 2019

PubMed Abstract: Plant tyrosine decarboxylase (TyrDC) is a group II pyridoxal 5'-phosphate (PLP)-dependent decarboxylase that mainly catalyzes the decarboxylation of tyrosine to tyramine. This is biologically important for diverting essential primary metabolites into secondary metabolic pathways. Intensive studies have characterized the effective of PLP-binding and the substrate specificity of mammalian 3,4-dihydroxyphenyl-l-alanine (Dopa) decarboxylases, a member of group II PLP-dependent decarboxylase. However, the characteristics of PLP binding and substrate specificity of plant TyrDCs remain unknown. In this study, we focus on the PLP binding manner, and determined the crystal structures of the apo and PLP binding form of type II TyrDC from Papaver somniferum (PsTyrDCII and PsTyrDCII-PLP). The structures showed that, unlike mammalian Dopa decarboxylase, the binding of PLP does not induce distinct conformational changes of PsTyrDCII regarding the overall structure, but the PLP binding pocket displays conformational changes at Phe124, His203 and Thr262. Combining structural comparation and the obtained biochemical findings, it is demonstrated that PsTyrDCII does not binds PLP tightly. Such characteristics of PLP binding may be required by its catalytic reaction and substrate binding. The activity of TyrDC probably regulated by the concentration of PLP in cells.

PubMed: 31898973
DOI: 10.1016/j.bbrc.2019.12.077

実験手法

X-RAY DIFFRACTION (2.8 Å)