8i28
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae== | |
| + | <StructureSection load='8i28' size='340' side='right'caption='[[8i28]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8i28]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8I28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I28 FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8i28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i28 OCA], [https://pdbe.org/8i28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i28 RCSB], [https://www.ebi.ac.uk/pdbsum/8i28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i28 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SERC_YEAST SERC_YEAST] Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.[UniProtKB:Q96255] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 A. 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. | ||
| - | + | Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae.,Jang J, Chang JH Int J Mol Sci. 2023 Mar 7;24(6):5139. doi: 10.3390/ijms24065139. PMID:36982214<ref>PMID:36982214</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8i28" style="background-color:#fffaf0;"></div> |
| - | [[Category: Chang | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Chang JH]] | ||
| + | [[Category: Jang JY]] | ||
Revision as of 07:34, 3 May 2023
Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae
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