Figure 4

Ribbon presentation of predicted structures of Bleg1_2507 with extended N-terminus and Bleg1_2337. (A) Generated model of Bleg1_2507 exhibiting Trx-like global topology, with the presence of four α-helices (cyan) and eight β-sheets (magenta) (B) The distances between S of Cys-69 and Cys-73 with Nϵ2 and Nδ1 of His-159 were ~16.4 and ~17.5 Å respectively, which are considered far for metallation process in the predicted Sco protein Bleg1_2507 with the presence of hydrophobic residues on the loop 4 and loop 9 (color-coded and numerically weight hydrophobicity based on [26]) (C) Generated model of Bleg1_2337 with a β-sheets cluster at the core of the protein surrounded by 10 α-helices. α1, α2, α3 and α4 form an extended arm which allowed interaction with Bleg1_2507, the predicted Sco protein (D) Hydrophobic residues (color-coded and numerically weight hydrophobicity based on [26]) of Bleg1_2337 that might be involved in the interaction with predicted Sco (Bleg1_2507) during metallation process and electron transfer.