Succinimide confers structural stability to MjGATase

Succinimide confers structural stability to MjGATase

Our studies on M. jannaschii (Mj) GATase, has led to the finding of a remarkably stable succinimide that plays a critical role in conferring hyperthermostability to the protein. Due to the high susceptibility of succinimides to hydrolysis leading to the formation of beta-aspartyl residues, this post-translational modification is generally associated with destabilization ofprotein structure and thereby, age associated disorders in humans. Our findings on Mj GATase that is contradictory to the existing understanding of succinimides opens up a novel mode for enhancing protein stability.

a. Molar ellipticity at 220 nm as a function of temperature of Wild type and  mutants of MjGATase 
b.Effect of boiling on mutants and wild-type MjGATase