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

Okoda, N.; Okuda, S.; Tsutsumi, K.; Itoh, H.; Okamoto, K.; Kawakami, H.; Sano, K.; Kobata, K.; Nagata, K.

doi:10.1107/S2053230X26003456

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
Crystal structure of A. thaliana GABA aminotransferase (AtGABA-T). (a) Structural overview of the AtGABA-T dimers (chains A–B and C–D) observed in the crystal lattice. The PLP cofactor is covalently linked to Lys292 in all subunits, forming an internal aldimine. PLP and Lys292 are shown as yellow spheres. (b) Close-up view of the active site showing the internal aldimine form of PLP. The main protomer is shown in green and the neighboring protomer is shown in cyan. A polder map contoured at 4.0σ is shown around the PLP cofactor.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 82| Part 6| June 2026| Pages 208-215

https://doi.org/10.1107/S2053230X26003456

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