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 language | English (US) |
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Pages (from-to) | 930-933 |
Number of pages | 4 |
Journal | Protein Science |
Volume | 8 |
Issue number | 4 |
DOIs | |
State | Published - 1999 |
Externally published | Yes |
Keywords
- Dimer interface
- Disulfide engineering
- Stability
- Thymidylate synthase
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology