Crystal structure of methylesterase family member 16 (MES16) from Arabidopsis thaliana.
Methylesterase family member 16 (MES16) is an integral component of chlorophyll breakdown. It catalyzes the demethylation of fluorescent chlorophyll catabolite (FCC) and pheophorbide in vitro, and specifically demethylates FCC in vivo. Here we report the crystal structure of MES16 from Arabidopsis thaliana at 2.8 Å resolution. The structure confirm that MES16 is a member of the α/β-hydrolase superfamily with Ser-87, His-239, and Asp-211 as the catalytic triad. Our biochemical studies reveal that MES16 has esterase activity with methyl-indole acetic acid as the substrate, and the catalytically essential role of Ser-87 has been demonstrated.
Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing, 100093, People's Republic of China. Electronic address: hmli@ibcas.ac.cn.
Hongmei
H
Li
Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing, 100093, People's Republic of China; University of Chinese Academy of Sciences, College of Life Science, Beijing, 101048, People's Republic of China.
Hua
H
Pu
D017360:Arabidopsis / Q000201:enzymology*; D001665:Binding Sites; D004789:Enzyme Activation; D007210:Indoleacetic Acids / Q000737:chemistry*; D008780:Methyltransferases / Q000737:chemistry* / Q000648:ultrastructure*; D011485:Protein Binding; D011487:Protein Conformation
D007210:Indoleacetic Acids; D008780:Methyltransferases
Arabidopsis thaliana; Catalytic triad; Chlorophyll breakdown; Demethylation; MES16; α/β-hydrolase superfamily