Fig. 3.

Superposition of the active site motif from different thioredoxins and Stereo surface representation of CnTrx1 monomer. (a) Trxs C. neoformans monomer B (orange, PDB ID: 5JY5), M. sympodialys (blue, PDB ID: 2J23), S. cerevisiae (purple, PDB ID: 2OE0), L. vannamei (green, PDB ID: 4AJ6), H. Sapiens (pink, PDB ID: 5DQY) and E. coli (gray, PDB ID: 1XOA). The overlay shows the conservation around the cysteines and the position of water molecules bound to Asp. The distances indicated between the internal water molecule with Asp²⁴ and Cys³³ are for the CnTrx1. (b) Superposition of CnTrx1_ox monomers A (green) and B (pink) with the side chains of Trp²⁹, Cys³⁰ and Cys³³ side chains shown in stick. The distances between C_α atoms of the two monomers in the loop region prior to helix α2 are depicted by black dashes and given in Å. (c) Two 180° apart views of the CnTrx1 electrostatic surface potentials (red, negative; blue, positive) as calculated with the GRASP Poisson-Boltzmann [58]. The disulfide bond (Cys³⁰-Cys³³) surface was omitted to facilitate viewing. The charged amino acid residues are pointed out by their type and sequence number. The figures were made using PyMOL.