4d7l | pdb_00004d7l

Methionine sulfoxide reductase A of Corynebacterium diphtheriae

spinqualitylabelsall models 4d7l, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d7l is a 3 chain structure with sequence from Corynebacterium diphtheriae NCTC 13129. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.895Å Ligands: CAC, PGE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MSRA_CORDI Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. Publication Abstract from PubMed Methionine sulfoxide reductases are conserved enzymes that reduce oxidized methionines in proteins, and play a pivotal role in cellular redox signaling. We have unraveled the redox relay mechanisms of methionine sulfoxide reductase A of the pathogen C. diphtheria (Cd-MsrA), and showed that this enzyme is coupled to two independent redox relay pathways. Steady-state kinetics combined with mass spectrometry of Cd-MsrA mutants give a view of the essential cysteine residues for catalysis. Cd-MsrA combines a nucleophilic cysteine sulfenylation reaction with an intramolecular disulfide bond cascade linked to the thioredoxin pathway. Within this cascade, the oxidative equivalents are transferred to the surface of the protein, while releasing the reduced substrate. Alternatively, MsrA catalyzes methionine sulfoxide reduction linked to the mycothiol/mycoredoxin-1 pathway. After the nucleophilic cysteine sulfenylation reaction, MsrA forms a mixed disulfide with mycothiol, which is transferred via a thiol disulfide relay mechanism to a second cysteine for reduction by mycoredoxin-1. With X-ray crystallography, we visualize two essential intermediates of the thioredoxin relay mechanism, and a cacodylate molecule mimicking the substrate interactions in the active site. The interplay of both redox pathways in redox signaling regulation forms the basis for further research into the oxidative stress response of this pathogen. Corynebacterium diphtheriae methionine sulfoxide reductase A exploits a unique mycothiol redox relay mechanism.,Tossounian MA, Pedre B, Wahni K, Erdogan H, Vertommen D, Van Molle I, Messens J J Biol Chem. 2015 Mar 9. pii: jbc.M114.632596. PMID:25752606 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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