7DLY

Crystal structure of Arabidopsis ACS7 mutant in complex with PPG

7DLY の概要

• エントリーDOI: 10.2210/pdb7dly/pdb
• 関連するPDBエントリー: 7DLW
• 分子名称: 1-aminocyclopropane-1-carboxylate synthase 7, (2E,3E)-4-(2-aminoethoxy)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid (2 entities in total)
• 機能のキーワード: acc synthetase, ethylene, plant protein, lyase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102017.11

構造登録者

Hao, B.,Zhang, Y.,Li, X.,Rao, Z. (登録日: 2020-11-30, 公開日: 2021-09-29, 最終更新日: 2023-11-29)

主引用文献

Xu, C.,Hao, B.,Sun, G.,Mei, Y.,Sun, L.,Sun, Y.,Wang, Y.,Zhang, Y.,Zhang, W.,Zhang, M.,Zhang, Y.,Wang, D.,Rao, Z.,Li, X.,Shen, Q.J.,Wang, N.N.
Dual activities of ACC synthase: Novel clues regarding the molecular evolution of ACS genes.
Sci Adv, 7:eabg8752-eabg8752, 2021

PubMed Abstract: Ethylene plays profound roles in plant development. The rate-limiting enzyme of ethylene biosynthesis is 1-aminocyclopropane-1-carboxylate (ACC) synthase (ACS), which is generally believed to be a single-activity enzyme evolving from aspartate aminotransferases. Here, we demonstrate that, in addition to catalyzing the conversion of -adenosyl-methionine to the ethylene precursor ACC, genuine ACSs widely have C-S lyase activity. Two N-terminal motifs, including a glutamine residue, are essential for conferring ACS activity to ACS-like proteins. Motif and activity analyses of ACS-like proteins from plants at different evolutionary stages suggest that the ACC-dependent pathway is uniquely developed in seed plants. A putative catalytic mechanism for the dual activities of ACSs is proposed on the basis of the crystal structure and biochemical data. These findings not only expand our current understanding of ACS functions but also provide novel insights into the evolutionary origin of genes.

PubMed: 34757795
DOI: 10.1126/sciadv.abg8752

実験手法

X-RAY DIFFRACTION (2.94 Å)