Extended Data Fig. 8: Superposition of NgTAL in the oxidized and reduced state. | Nature

Extended Data Fig. 8: Superposition of NgTAL in the oxidized and reduced state.

From: A lysine–cysteine redox switch with an NOS bridge regulates enzyme function

Extended Data Fig. 8

Both of these structures are from this Article. a, Structure of the active site of NgTAL in the oxidized state, showing catalytic residues Lys138, Asp17 and the ligand citrate. Citrate is partially disordered. The corresponding 2mFo − DFc (blue) and mFo − DFc omit (green) electron density maps are shown at contour levels of 1σ and 5σ, respectively. b, Structure of the active site of NgTAL in the reduced state, showing catalytic residues Lys138, Asp17 and the ligand citrate. Citrate is structurally well-defined in this state. A covalent conjugate between Lys138 and a two-carbon fragment formed during crystallization. The corresponding 2mFo − DFc (blue) and mFo − DFc omit (green) electron density maps are shown at contour levels of 1σ and 5σ, respectively. c, Superposition of the oxidized (yellow) and reduced (grey) NgTAL, showing selected active site residues and the ligand citrate. The structural change of ligand citrate is accompanied by a redistribution of the two conformers of Arg204 (oxidized 70:30% occupancy, reduced 30:70% occupancy). There is also a subtle repositioning of the active-site residues (for example, Asp17 and water molecules).

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