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May 3, 2026

Crystal structure of the plant GABA aminotransferase AtGABA-T from Arabidopsis thaliana.

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Authors

NONaofumi OkodaSOSuguru OkudaKTKenta Tsutsumi

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Overview

Crystal structure reveals unique substrate recognition mechanism in plant GABA aminotransferase AtGABA-T.

Key Points

  • The study aims to elucidate the crystal structure and substrate recognition mechanism of AtGABA-T.
  • Determined the crystal structure of AtGABA-T from Arabidopsis thaliana at 2.0 Å resolution.
  • Used Foldseek for structural comparison with other aminotransferases.
  • Identified key residues involved in substrate recognition.
  • AtGABA-T is classified as a class III aminotransferase based on structural characteristics.
  • The C-terminal arginine (Arg423) is crucial for GABA recognition, differing from nonplant GABA-Ts.
  • Findings suggest a distinct substrate-access pathway compared to mammalian and bacterial homologs.

Cite This Study

Okoda et al. (2026) studied this question.

synapsesocial.com/papers/69f6e67c8071d4f1bdfc721bhttps://doi.org/10.1107/s2053230x26003456
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