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Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae

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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Autores principales: Jang, Jiyeon, Chang, Jeong Ho
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10049462/
https://www.ncbi.nlm.nih.gov/pubmed/36982214
http://dx.doi.org/10.3390/ijms24065139
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author Jang, Jiyeon
Chang, Jeong Ho
author_facet Jang, Jiyeon
Chang, Jeong Ho
author_sort Jang, Jiyeon
collection PubMed
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 Saccharomyces cerevisiae PSAT (ScPSAT) at a resolution of 2.8 Å. The results demonstrated that the ScPSAT protein was dimeric in its crystal structure. Moreover, the gate-keeping loop of ScPSAT exhibited a conformation similar to that of other species. Several distinct structural features in the halide-binding and active sites of ScPSAT 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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spelling pubmed-100494622023-03-29 Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae Jang, Jiyeon Chang, Jeong Ho Int J Mol Sci Article 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 Saccharomyces cerevisiae PSAT (ScPSAT) at a resolution of 2.8 Å. The results demonstrated that the ScPSAT protein was dimeric in its crystal structure. Moreover, the gate-keeping loop of ScPSAT exhibited a conformation similar to that of other species. Several distinct structural features in the halide-binding and active sites of ScPSAT 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. MDPI 2023-03-07 /pmc/articles/PMC10049462/ /pubmed/36982214 http://dx.doi.org/10.3390/ijms24065139 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Jang, Jiyeon
Chang, Jeong Ho
Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae
title Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae
title_full Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae
title_fullStr Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae
title_full_unstemmed Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae
title_short Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae
title_sort molecular structure of phosphoserine aminotransferase from saccharomyces cerevisiae
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10049462/
https://www.ncbi.nlm.nih.gov/pubmed/36982214
http://dx.doi.org/10.3390/ijms24065139
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