Figure 1: Structural features of PfTET3.
From: Tuned by metals: the TET peptidase activity is controlled by 3 metal binding sites
(A) PfTET3 trimer in the asymmetric unit. The three monomers are almost identical with an r.m.s.d of 0.18 Å over the three chains. (B) PfTET3 dodecameric assembly obtained by applying the symmetry operators. Each trimer is highlighted by a different color (violet, green, yellow and cyan). Grey spheres represents metal ions. The sticks represent the DO3A bound to the Gd atoms. (C) Dinuclear active site and specificity binding pocket of one monomer. M1 site is coordinated by Asp177, Glu208 and His314 and M2 site is coordinated by His63, Asp177 and Asp230 (grey spheres). The identity of each metal ion is unknown. The specificity binding pocket is formed by Thr232, Asp254 and Glu281. (D) Zoom of the dinuclear metal center. Grey spheres are M1 and M2, gold sphere is Cl− and ice blue spheres are water molecules. M1 has an octahedral geometry while M2 has a trigonal bipyramidal geometry.
