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...
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MDPI AG
2023-03-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/6/5139 |
| _version_ | 1797611364306386944 |
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| author | Jiyeon Jang Jeong Ho Chang |
| author_facet | Jiyeon Jang Jeong Ho Chang |
| author_sort | Jiyeon Jang |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-11T06:26:49Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T06:26:49Z |
| publishDate | 2023-03-01 |
| publisher | MDPI AG |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-2ababa2f885a41a0a701304f0826afdb2023-11-17T11:29:38ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-03-01246513910.3390/ijms24065139Molecular Structure of Phosphoserine Aminotransferase from <i>Saccharomyces cerevisiae</i>Jiyeon Jang0Jeong Ho Chang1Department of Biology Education, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Republic of KoreaDepartment of Biology Education, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Republic of KoreaPhosphoserine 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.https://www.mdpi.com/1422-0067/24/6/5139phosphoserine aminotransferaseprotein crystallography<i>Saccharomyces cerevisiae</i>phylogenetic relationshipcrystal structurepyridoxal 5′-phosphate |
| spellingShingle | Jiyeon Jang Jeong Ho Chang Molecular Structure of Phosphoserine Aminotransferase from <i>Saccharomyces cerevisiae</i> International Journal of Molecular Sciences phosphoserine aminotransferase protein crystallography <i>Saccharomyces cerevisiae</i> phylogenetic relationship crystal structure pyridoxal 5′-phosphate |
| title | Molecular Structure of Phosphoserine Aminotransferase from <i>Saccharomyces cerevisiae</i> |
| title_full | Molecular Structure of Phosphoserine Aminotransferase from <i>Saccharomyces cerevisiae</i> |
| title_fullStr | Molecular Structure of Phosphoserine Aminotransferase from <i>Saccharomyces cerevisiae</i> |
| title_full_unstemmed | Molecular Structure of Phosphoserine Aminotransferase from <i>Saccharomyces cerevisiae</i> |
| title_short | Molecular Structure of Phosphoserine Aminotransferase from <i>Saccharomyces cerevisiae</i> |
| title_sort | molecular structure of phosphoserine aminotransferase from i saccharomyces cerevisiae i |
| topic | phosphoserine aminotransferase protein crystallography <i>Saccharomyces cerevisiae</i> phylogenetic relationship crystal structure pyridoxal 5′-phosphate |
| url | https://www.mdpi.com/1422-0067/24/6/5139 |
| work_keys_str_mv | AT jiyeonjang molecularstructureofphosphoserineaminotransferasefromisaccharomycescerevisiaei AT jeonghochang molecularstructureofphosphoserineaminotransferasefromisaccharomycescerevisiaei |