8p1z | pdb_00008p1z

Arabidopsis thaliana cytosolic seryl-tRNA synthetase in addition of dithiothreitol (DTT)

spinqualitylabelsall models 8p1z, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8p1z is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SYSC_ARATH Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).[UniProtKB:P0A8L1] Publication Abstract from PubMed 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(2) O(2) , 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. Evolutionarily conserved cysteines in plant cytosolic seryl-tRNA synthetase are important for its resistance to oxidation.,Evic V, Soic R, Mocibob M, Kekez M, Houser J, Wimmerova M, Matkovic-Calogovic D, Gruic-Sovulj I, Kekez I, Rokov-Plavec J FEBS Lett. 2023 Dec;597(23):2975-2992. doi: 10.1002/1873-3468.14748. Epub 2023 , Oct 10. PMID:37804069 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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