Dams, T. and Boehm, G. and Auerbach, G. and Bader, G. and Schurig, H. and Jaenicke, Rainer (1998) Homo-dimeric recombinant dihydrofolate reductase from Thermotoga maritima shows extreme intrinsic stability. BIOLOGICAL CHEMISTRY, 379 (3). pp. 367-371. ISSN 1431-6730,
Full text not available from this repository.Abstract
Dihydrofolate reductase (DHFR) from the hyperthermophilic bacterium Thermotoga maritima was cloned and expressed in Escherichia coli. Sequence determination of the reported dyrA gene was repeated, and a corrected version deposited in the nucleotide sequence databank (accession number Y11021). Urtracentrifugational analysis and gel permeation chromatography prove that the enzyme forms a stable homodimer. The enzyme exhibits long-term stability at physiological temperature (80 degrees C) and in the presence of high denaturant concentrations (half-time in 6 M guanidinium chloride: 24 h). Alignments of DHFRS from different species, as well as comparative modeling based on the homology to the crystal structures of the enzyme from prokaryotes and eukaryotes, were used to generate a model of the three-dimensional structure. The apoenzyme was crystallized and a data set was collected to a resolution of about 2 Angstrom.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ESCHERICHIA-COLI; LACTATE-DEHYDROGENASE; SUBSTRATE BINDING; PROTEIN; ISOMERASE; ENOLASE; GENE; NMR; crystallization; comparative modeling; dihydrofolate reductase; dimer; thermostability; Thermotoga maritima |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 12 Sep 2023 09:21 |
| Last Modified: | 12 Sep 2023 09:21 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50030 |
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