Molecular Structure of Phosphoserine Aminotransferase from <i>Saccharomyces cerevisiae</i>
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 structu...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-03-01
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| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/24/6/5139 |
| Summary: | 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 <i>Saccharomyces cerevisiae</i> PSAT (<i>Sc</i>PSAT) at a resolution of 2.8 Å. The results demonstrated that the <i>Sc</i>PSAT protein was dimeric in its crystal structure. Moreover, the gate-keeping loop of <i>Sc</i>PSAT exhibited a conformation similar to that of other species. Several distinct structural features in the halide-binding and active sites of <i>Sc</i>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. |
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| ISSN: | 1661-6596 1422-0067 |