8I28

Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae

8I28 の概要

• エントリーDOI: 10.2210/pdb8i28/pdb
• 分子名称: Phosphoserine aminotransferase (2 entities in total)
• 機能のキーワード: phosphoserine, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 86940.86

構造登録者

Jang, J.Y.,Chang, J.H. (登録日: 2023-01-14, 公開日: 2023-05-03, 最終更新日: 2024-05-29)

主引用文献

Jang, J.,Chang, J.H.
Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae.
Int J Mol Sci, 24:-, 2023

PubMed Abstract: 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.

PubMed: 36982214
DOI: 10.3390/ijms24065139

実験手法

X-RAY DIFFRACTION (2.8 Å)