8P1Y
Arabidopsis thaliana mutated variant C244S of seryl-tRNA synthetase
This is a non-PDB format compatible entry.
Summary for 8P1Y
| Entry DOI | 10.2210/pdb8p1y/pdb |
| Descriptor | Serine--tRNA ligase, cytoplasmic (2 entities in total) |
| Functional Keywords | synthetase, class ii, cytoplasmic, cytosolic protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 52127.24 |
| Authors | Kekez, I.,Soic, R.,Rokov-Plavec, J.,Matkovic-Calogovic, D. (deposition date: 2023-05-13, release date: 2024-05-22, Last modification date: 2024-12-04) |
| Primary citation | Evic, V.,Soic, R.,Mocibob, M.,Kekez, M.,Houser, J.,Wimmerova, M.,Matkovic-Calogovic, D.,Gruic-Sovulj, I.,Kekez, I.,Rokov-Plavec, J. Evolutionarily conserved cysteines in plant cytosolic seryl-tRNA synthetase are important for its resistance to oxidation. Febs Lett., 597:2975-2992, 2023 Cited by PubMed Abstract: We have previously identified a unique disulfide bond in the crystal structure of Arabidopsis cytosolic seryl-tRNA synthetase involving cysteines evolutionarily conserved in all green plants. Here, we discovered that both cysteines are important for protein stability, but with opposite effects, and that their microenvironment may promote disulfide bond formation in oxidizing conditions. The crystal structure of the C244S mutant exhibited higher rigidity and an extensive network of noncovalent interactions correlating with its higher thermal stability. The activity of the wild-type showed resistance to oxidation with H O , while the activities of cysteine-to-serine mutants were impaired, indicating that the disulfide link may enable the protein to function under oxidative stress conditions which can be beneficial for an efficient plant stress response. PubMed: 37804069DOI: 10.1002/1873-3468.14748 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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