4emj

Complex between the reductase and ferredoxin components of toluene dioxygenase

spinqualitylabelsall models 4emj, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4emj is a 2 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: FAD, FES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TODA_PSEP1 Part of the electron transfer component of toluene 1,2-dioxygenase, transfers electrons from ferredoxin (TodB) to NADH. Publication Abstract from PubMed The three-component toluene dioxygenase system consists of an FAD-containing reductase, a Rieske-type [2Fe-2S] ferredoxin, and a Rieske-type dioxygenase. The task of the FAD-containing reductase is to shuttle electrons from NADH to the ferredoxin, a reaction the enzyme has to catalyze in the presence of dioxygen. We investigated the kinetics of the reductase in the reductive and oxidative half-reaction and detected a stable charge transfer complex between the reduced reductase and NAD(+) at the end of the reductive half-reaction, which is substantially less reactive toward dioxygen than the reduced reductase in the absence of NAD(+). A plausible reason for the low reactivity toward dioxygen is revealed by the crystal structure of the complex between NAD(+) and reduced reductase, which shows that the nicotinamide ring and the protein matrix shield the reactive C4a position of the isoalloxazine ring and force the tricycle into an atypical planar conformation, both factors disfavoring the reaction of the reduced flavin with dioxygen. A rapid electron transfer from the charge transfer complex to electron acceptors further reduces the risk of unwanted side reactions, and the crystal structure of a complex between the reductase and its cognate ferredoxin shows a short distance between the electron-donating and -accepting cofactors. Attraction between the two proteins is likely mediated by opposite charges at one large patch of the complex interface. The stability, specificity, and reactivity of the observed charge transfer and electron transfer complexes are thought to prevent the reaction of reductase(TOL) with dioxygen and thus present a solution toward conflicting requirements. Suppression of Electron Transfer to Dioxygen by Charge Transfer and Electron Transfer Complexes in the FAD-dependent Reductase Component of Toluene Dioxygenase.,Lin TY, Werther T, Jeoung JH, Dobbek H J Biol Chem. 2012 Nov 2;287(45):38338-46. doi: 10.1074/jbc.M112.374918. Epub 2012, Sep 19. PMID:22992736 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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