Characterization of a novel cysteine-less Cu/Zn-superoxide dismutase in Paenibacillus lautus missing a conserved disulfide bond

被引：1

作者：

Furukawa, Yoshiaki ^{[1
]}

Shintani, Atsuko ^{[1
]}

Narikiyo, Shuhei ^{[1
]}

Sue, Kaori ^{[1
]}

Akutsu, Masato ^{[1
]}

Muraki, Norifumi ^{[1
]}

机构：

[1] Keio Univ, Dept Chem, Yokohama, Japan

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2023年 / 299卷 / 08期

关键词：

FAMILIAL FORM; COPPER; SOD1; STABILITY; PATHWAYS; ACID; CU;

D O I：

10.1016/j.jbc.2023.105040

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页数：13

共 51 条

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