Skip to main content Accessibility help
×
Home

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

  • S.S. VELANKER (a1), R.S. GOKHALE (a1), SOUMYA S. RAY (a1), B. GOPAL (a1), S. PARTHASARATHY (a1), D.V. SANTI (a2), P. BALARAM (a1) (a3) and M.R.N. MURTHY (a1)...

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.

Copyright

Corresponding author

Reprint requests to: M.R.N. Murthy, Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India; e-mail: mrn@mbu.iisc.ernet.in.

Keywords

Related content

Powered by UNSILO

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

  • S.S. VELANKER (a1), R.S. GOKHALE (a1), SOUMYA S. RAY (a1), B. GOPAL (a1), S. PARTHASARATHY (a1), D.V. SANTI (a2), P. BALARAM (a1) (a3) and M.R.N. MURTHY (a1)...

Metrics

Full text views

Total number of HTML views: 0
Total number of PDF views: 0 *
Loading metrics...

Abstract views

Total abstract views: 0 *
Loading metrics...

* Views captured on Cambridge Core between <date>. This data will be updated every 24 hours.

Usage data cannot currently be displayed.