Crystal structure of manganese catalase from Lactobacillus plantarum

Background: Catalases are important antioxidant metalloenzymes that catalyz e disproportionation of hydrogen peroxide, forming dioxygen and water. Two families of catalases are known, one having a heme cofactor, and the other, a structurally distinct family containing nonheme manganese. We have solve d the structure of the mesophilic manganese catalase from Lactobacillus pla ntarum and its azide-inhibited complex. Results: The crystal structure of the native enzyme has been solved at 1.8 Angstrom resolution by molecular replacement, and the azide complex of the native protein has been solved at 1.4 Angstrom resolution. The hexameric st ructure of the holoenzyme is stabilized by extensive intersubunit contacts, including a beta zipper and a structural calcium ion crosslinking neighbor ing subunits. Each subunit contains a dimanganese active site, accessed by a single substrate channel lined by charged residues. The manganese ions ar e linked by a mu (1,3)-bridging glutamate carboxylate and two mu -bridging solvent oxygens that electronically couple the metal centers. The active si te region includes two residues (Arg147 and Glu178) that appear to be uniqu e to the Lactobacillus plantarum catalase. Conclusions: A comparison of L. plantarum and T. thermophilus catalase stru ctures reveals the existence of two distinct structural classes, differing in monomer design and the organization of their active sites, within the ma nganese catalase family. These differences have important implications for catalysis and may reflect distinct biological functions for the two enzymes , with the L. plantarum enzyme serving as a catalase, while the T. thermoph ilus enzyme may function as a catalase/peroxidase.