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

S. S. Velanker, R. S. Gokhale, Soumya S. Ray, B. Gopal, S. Parthasarathy, D. V. Santi, P. Balaram, M. R.N. Murthy

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Abstract

The crystal structure of a covalently cross-linked Lactobacillus casei thymidylate synthase has been determined at 2.8 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.

Original languageEnglish (US)
Pages (from-to)930-933
Number of pages4
JournalProtein Science
Volume8
Issue number4
Publication statusPublished - Jan 1 1999

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Keywords

  • Dimer interface
  • Disulfide engineering
  • Stability
  • Thymidylate synthase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Velanker, S. S., Gokhale, R. S., Ray, S. S., Gopal, B., Parthasarathy, S., Santi, D. V., ... Murthy, M. R. N. (1999). Disulfide engineering at the dimer interface of Lactobacillus casei thymidylate synthase: Crystal structure of the T155C/E188C/C244T mutant. Protein Science, 8(4), 930-933.