Formation of high-order oligomers by a hyperthemostable Fe-superoxide dismutase (tcSOD).

ABSTRACT: Hyperthermostable proteins are highly resistant to various extreme conditions. Many factors have been proposed to contribute to their ultrahigh structural stability. Some thermostable proteins have larger oligomeric size when compared to their mesophilic homologues. The formation of compact oligomers can minimize the solvent accessible surface area and increase the changes of Gibbs free energy for unfolding. Similar to mesophilic proteins, hyperthermostable proteins also face the problem of unproductive aggregation. In this research, we investigated the role of high-order oligomerization in the fight against aggregation by a hyperthermostable superoxide dismutase identified from Tengchong, China (tcSOD). Besides the predominant tetramers, tcSOD could also form active high-order oligomers c

SUBMITTER: Wang S 

PROVIDER: S-EPMC4196948 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature