6a4j | pdb_00006a4j

Crystal structure of Thioredoxin reductase 2 from Staphylococcus aureus

spinqualitylabelsall models 6a4j, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6a4j is a 2 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. This structure supersedes the now removed PDB entry 5zbv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD Gene: trxB_2, EP54_04310, EQ90_00075, RK60_12235, RK64_12650, RK68_02995, RK73_09520, RK98_08250, RL06_05030, SAMEA3448991_00661 ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885) Activity: Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The redox homeostasis of cytoplasm is maintained by a series of disulfide exchange reactions mediated by proteins belonging to the thioredoxin superfamily. Thioredoxin and thioredoxin reductase, being the major members of the family, play a key role in oxidative stress response of Staphylococcus aureus. In this report, we have identified and characterised an active thioredoxin system of the mentioned pathogen. Crystal structure of thioredoxin2 (SaTrx2) in its reduced form reveals that it contains the conserved redox active WCXXC motif and a thioredoxin fold. Thioredoxin reductase2 (SaTR2) is a flavoprotein and consists of two Rossmann folds as the binding sites for FAD and NADPH. Crystal structure of the SaTR2 holoenzyme shows that the protein consists of two domains and the catalytic site comprises of an intramolecular disulfide bond formed between two sequentially distal cysteine residues. Biophysical and biochemical studies unveil that SaTrx2 and SaTR2 can physically interact in solution and in the course of sustaining the redox equilibrium, the latter reduces the former. Molecular docking has been performed to illustrate the interface formed between SaTrx2 and SaTR2 during the disulfide exchange reaction. Elucidation of the mechanism of disulfide exchange between staphylococcal thioredoxin2 and thioredoxin reductase2: A structural insight.,Bose M, Bhattacharyya S, Biswas R, Roychowdhury A, Bhattacharjee A, Ghosh AK, Das AK Biochimie. 2019 Jan 31;160:1-13. doi: 10.1016/j.biochi.2019.01.019. PMID:30710560 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thioredoxin Reductase

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