Figure 4
Structures of AaL and comparison to other known structures of MLLs. (A) AaL monomer shows a αβ/βα fold that contains two metal cations (pink spheres) and a bound phosphate anion (orange sticks). The α-helices, β-sheets and loops are represented in red, yellow and green, respectively. (B) AaL dimer. Each monomer (in blue and gold) contains an active site with two cobalt cations (pink spheres) bound to a phosphate anion (orange sticks). (C) Comparison of AaL (grey) and AiiA (pink) monomers. (D) Superposition of AaL dimer (grey) with the AiiA (pink) monomer. (E) Superposition of the monomers AaL (grey) and AiiB (green). (F) Comparison of the dimers of AaL (grey) and AiiB (green). The two enzymes show a similar dimerization mode. (G) Superposition of the monomer of AaL (grey) and AidC (cyan). (H) Superposition of AaL (grey) and AidC (cyan) dimers reveals their use of a different dimerization interface.
