Direct relationship between dimeric form and activity in the acidic copper-zinc superoxide dismutase from lemon.

ABSTRACT: The copper-zinc superoxide dismutase (CuZnSOD) from lemon (SOD_CL) is active in an acidic environment and resists proteolytic degradation. The enzyme occurs as a dimer, which has an indirect effect on the enzyme activity as the monomer retains only ∼35% of the activity. Here, the crystal structure of SOD_CL at 1.86 Å resolution is reported that may explain this peculiarity. The crystal belonged to space group P2₁, with unit-cell parameters a = 61.11, b = 74.55, c = 61.69 Å, β = 106.86°, and contained four molecules in the asymmetric unit. The overall structure of SOD_CL resembles that of CuZnSOD from plants. The structure of SOD_CL shows a unique arrangement of surface loop IV that connects the dimer interface and the active site, which is located away from the dimer-interface r

SUBMITTER: Utami RA 

PROVIDER: S-EPMC10833119 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature