ArticleActa crystallographica. Section F, Structural biology communications2026
Crystal structure of the plant GABA aminotransferase AtGABA-T from Arabidopsis thaliana.
Article in Acta crystallographica. Section F, Structural biology communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
γ-Aminobutyric acid aminotransferase (GABA-T) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes γ-aminobutyric acid (GABA) degradation in the mitochondrial GABA shunt. Plant GABA-Ts correspond to EC 2.6.1.96 and differ from mammalian and bacterial GABA-Ts (EC 2.6.1.19) in substrate specificity; however, their structural basis has remained unclear. Here, we report the crystal structure of GABA aminotransferase from Arabidopsis thaliana (AtGABA-T) at 2.0 Å resolution. Structural comparison using Foldseek indicates that AtGABA-T belongs to the class III aminotransferase family. Comparison with a class III ω-aminotransferase suggests that Arg423 located in the C-terminal region of AtGABA-T functions as the primary anchor for the carboxyl group of GABA, together with residues forming a tunnel-shaped substrate-access pathway. In contrast to nonplant GABA aminotransferases, which utilize a conserved N-terminal arginine for substrate recognition, AtGABA-T employs a distinct C-terminal arginine. These findings provide direct structural evidence for the classification of AtGABA-T as a class III aminotransferase and reveal a distinct mode of substrate recognition in AtGABA-T.
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