7DLY

Crystal structure of Arabidopsis ACS7 mutant in complex with PPG

Summary for 7DLY

• Entry DOI: 10.2210/pdb7dly/pdb
• Related: 7DLW
• Descriptor: 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)
• Functional Keywords: acc synthetase, ethylene, plant protein, lyase
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 2
• Total formula weight: 102017.11

Authors

Hao, B.,Zhang, Y.,Li, X.,Rao, Z. (deposition date: 2020-11-30, release date: 2021-09-29, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.94 Å)