FIGURE 2.

Structure of curacin A thioesterase. A, CurM TE polypeptide. The stereo ribbon diagram is colored as a rainbow from blue at the N terminus to red at the C terminus with the catalytic triad residues in stick form with a magenta C. B, topology diagram. CurM TE has an α/β-hydrolase fold in the core domain and a novel lid topology. Residues of the catalytic triad (Ser¹⁰⁰, Glu¹²⁴, and His²⁶⁶) are labeled. C, backbone trace of the CurM TE dimer viewed along the molecular dyad. Monomers are colored as a rainbow (right) and in yellow (left), with the catalytic triad as in A, and N and C termini shown as spheres of the same color as the terminal residue.