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Structural and biochemical characterization of mitochondrial citrate synthase 4 from Arabidopsis thaliana
Author(s) -
Nishio Kazuya,
Mizushima Tsunehiro
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20001521
Subject(s) - citrate synthase , citric acid cycle , biochemistry , arabidopsis thaliana , mitochondrion , cofactor , coenzyme a , tricarboxylic acid , biology , metabolism , atp synthase , enzyme , atp citrate lyase , chemistry , gene , mutant , reductase
Citrate synthase (CS) catalyzes the conversion of oxaloacetate and acetyl coenzyme A into citrate and coenzyme A in the mitochondrial tricarboxylic acid (TCA) cycle. In plants, mitochondrial metabolism, including the TCA cycle, occurs in interaction with photosynthetic metabolism. The controlled regulation of several enzymes in the TCA cycle, such as CS, is important in plants. Here, the first crystal structure of a plant mitochondrial CS, CSY4 from Arabidopsis thaliana ( At CSY4), has been determined. Structural comparison of At CSY4 with mitochondrial CSs revealed a high level of similarity. Inhibition analysis showed a similar manner of inhibition as in mitochondrial CSs. The effect of oxidation on one of a pair of cysteine residues in At CSY4 was speculated upon based on the folded structure.