Velanker, S. S. ; Gokhale, R. S. ; Ray, Soumya S. ; Gopal, B. ; Parthasarathy, S. ; Santi, D. V. ; Balaram, P. ; 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). pp. 930-933. ISSN 0961-8368
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Official URL: http://www3.interscience.wiley.com/journal/1216012...
Related URL: http://dx.doi.org/10.1110/ps.8.4.930
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.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Cold Spring Harbor Laboratory Press. |
| Keywords: | Dimer Interface; Disulfide Engineering; Stability; Thymidylate Synthase |
| ID Code: | 4635 |
| Deposited On: | 18 Oct 2010 07:17 |
| Last Modified: | 16 May 2016 15:15 |
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