Disulfide engineering at the dimer interface of lactobacillus casei thymidylate synthase: crystal structure of the T155C/E188C/C244T mutant

Abstract

The crystal structure of a covalently cross-linked Lactobacillus casei thymidylate synthase has been determined at 2.8 å resolution. The sites for mutation to achieve the bis-disulfide linked dimer were identified using the disulfide modeling program MODIP. The mutant so obtained was found to be remarkably thermostable. This increase in stability has been reasoned to be entirely a consequence of the covalent gluing between the two subunits.