Department of Biology Education, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Republic of Korea.
Department of Biomedical Convergence Science and Technology, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Republic of Korea.
Int J Mol Sci. 2023 Mar 7;24(6):5139. doi: 10.3390/ijms24065139.
Phosphoserine aminotransferase (PSAT) is a pyridoxal 5'-phosphate-dependent enzyme involved in the second step of the phosphorylated pathway of serine biosynthesis. PSAT catalyzes the transamination of 3-phosphohydroxypyruvate to 3-phosphoserine using L-glutamate as the amino donor. Although structural studies of PSAT have been performed from archaea and humans, no structural information is available from fungi. Therefore, to elucidate the structural features of fungal PSAT, we determined the crystal structure of PSAT (PSAT) at a resolution of 2.8 Å. The results demonstrated that the PSAT protein was dimeric in its crystal structure. Moreover, the gate-keeping loop of PSAT exhibited a conformation similar to that of other species. Several distinct structural features in the halide-binding and active sites of PSAT were compared with its homologs. Overall, this study contributes to our current understanding of PSAT by identifying the structural features of fungal PSAT for the first time.
磷酸丝氨酸转氨酶（PSAT）是一种依赖于吡哆醛 5'-磷酸的酶，参与丝氨酸生物合成的磷酸化途径的第二步。PSAT 催化 3-磷酸羟丙酮酸与 L-谷氨酸之间的转氨基反应，生成 3-磷酸丝氨酸。尽管已经对古菌和人类的 PSAT 进行了结构研究，但真菌 PSAT 的结构信息尚不清楚。因此，为了阐明真菌 PSAT 的结构特征，我们解析了 PSAT（PSAT）的晶体结构，分辨率为 2.8Å。结果表明，PSAT 蛋白在晶体结构中呈二聚体形式。此外，PSAT 的门控环呈现出与其他物种相似的构象。还比较了 PSAT 卤化物结合和活性位点中的几个独特的结构特征与其同源物。总的来说，这项研究通过首次确定真菌 PSAT 的结构特征，有助于我们当前对 PSAT 的理解。
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