Ss. Velanker et al., Disulfide engineering at the dimer interface of Lactobacillus casei thymidylate synthase: Crystal structure of the T155C/E188C/C244T mutant, PROTEIN SCI, 8(4), 1999, pp. 930-933
The crystal structure of a covalently cross-linked Lactobacillus casei thym
idylate synthase has been determined at 2.8 Angstrom resolution. The sites
for mutation to achieve the bis-disulfide linked dimer were identified usin
g the disulfide modeling program MODIP. The mutant so obtained was found to
be remarkably thermostable. This increase in stability has been reasoned t
o be entirely a consequence of the covalent gluing between the two subunits
.