Figure 2 | Scientific Reports

Figure 2

From: Crystal structure of the hydroxylaminopurine resistance protein, YiiM, and its putative molybdenum cofactor-binding catalytic site

Figure 2

gsYiiM cavity as a putative catalytic site. (a) Electrostatic potential surface representation of the gsYiiM structure. The figure is viewed from the back of gsYiiM in the upper panel of Fig. 1a. (b) Surface representation of the gsYiiM structure that is color-coded by sequence conservation. The sequence conservation was calculated using the ConSurf server27. The invariant cysteine residue (C119) of gsYiiM is represented by a red circle. The orientation of gsYiiM in the figure is identical to that of gsYiiM in Fig. 2a. (c) Oxidized cysteine residue 119 (sulfur, a yellow sphere; oxygen, red spheres; carbon, light blue spheres) in the gsYiiM structure (green ribbons). The orientation of gsYiiM in the figure is identical to Fig. 2a. (d) Fo-Fc omit electron density map (gray wires shown in a 3.5σ level) for the sulfur atoms of four cysteine residues (C60, C98, C119, and C136; sticks) in the gsYiiM structure. The Sγ and Cβ atoms of the cysteine residues are vertically aligned.

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