8P1Y

Arabidopsis thaliana mutated variant C244S of seryl-tRNA synthetase

これはPDB形式変換不可エントリーです。

8P1Y の概要

• エントリーDOI: 10.2210/pdb8p1y/pdb
• 分子名称: Serine--tRNA ligase, cytoplasmic (2 entities in total)
• 機能のキーワード: synthetase, class ii, cytoplasmic, cytosolic protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52127.24

構造登録者

Kekez, I.,Soic, R.,Rokov-Plavec, J.,Matkovic-Calogovic, D. (登録日: 2023-05-13, 公開日: 2024-05-22, 最終更新日: 2024-12-04)

主引用文献

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

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: 37804069
DOI: 10.1002/1873-3468.14748

実験手法

X-RAY DIFFRACTION (2.6 Å)