8I28

Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae

Summary for 8I28

• Entry DOI: 10.2210/pdb8i28/pdb
• Descriptor: Phosphoserine aminotransferase (2 entities in total)
• Functional Keywords: phosphoserine, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 86940.86

Authors

Jang, J.Y.,Chang, J.H. (deposition date: 2023-01-14, release date: 2023-05-03, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)