8IMD

Crystal structure of Cu/Zn Superoxide dismutase from Paenibacillus lautus

Summary for 8IMD

• Entry DOI: 10.2210/pdb8imd/pdb
• Descriptor: Cu/Zn-Superoxide dismutase, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, COPPER (II) ION, ... (5 entities in total)
• Functional Keywords: superoxide dismutase, sod, sod1, oxidoreductase
• Biological source: Paenibacillus lautus NBRC 15380
• Total number of polymer chains: 2
• Total formula weight: 47183.57

Authors

Narikiyo, S.,Furukawa, Y.,Akutsu, M. (deposition date: 2023-03-06, release date: 2024-01-17)

Primary citation

Furukawa, Y.,Shintani, A.,Narikiyo, S.,Sue, K.,Akutsu, M.,Muraki, N.
Characterization of a novel cysteine-less Cu/Zn-superoxide dismutase in Paenibacillus lautus missing a conserved disulfide bond.
J.Biol.Chem., 299:105040-105040, 2023

PubMed Abstract: Cu/Zn-superoxide dismutase (CuZnSOD) is an enzyme that binds a copper and zinc ion and also forms an intramolecular disulfide bond. Together with the copper ion as the active site, the disulfide bond is completely conserved among these proteins; indeed, the disulfide bond plays critical roles in maintaining the catalytically competent conformation of CuZnSOD. Here, we found that a CuZnSOD protein in Paenibacillus lautus (PaSOD) has no Cys residue but exhibits a significant level of enzyme activity. The crystal structure of PaSOD revealed hydrophobic and hydrogen-bonding interactions in substitution for the disulfide bond of the other CuZnSOD proteins. Also notably, we determined that PaSOD forms a homodimer through an additional domain with a novel fold at the N terminus. While the advantages of lacking Cys residues and adopting a novel dimer configuration remain obscure, PaSOD does not require a disulfide-introducing/correcting system for maturation and could also avoid misfolding caused by aberrant thiol oxidations under an oxidative environment.

PubMed: 37442237
DOI: 10.1016/j.jbc.2023.105040

Experimental method

X-RAY DIFFRACTION (1.45 Å)