Auerbach, G. and Jacob, U. and Grattinger, M. and Schurig, H. and Jaenicke, Rainer (1997) Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium Thermotoga maritima. BIOLOGICAL CHEMISTRY, 378 (3-4). pp. 327-329. ISSN 1431-6730, 1437-4315
Full text not available from this repository.Abstract
Phosphoglycerate kinase from the hyperthermophilic bacterium Thermotoga maritima has been co-crystallized with its substrate 3-phosphoglycerate and the ATP analogue AMP-PNP using the vapour diffusion method. Crystals were obtained from a solution containing polyethylene glycol (MW 3000/8000) as precipitating agent. A complete diffraction data set from orthorhombic crystals was collected up to 2.0 Angstrom resolution. The TmPGK crystallizes in the space group P2(1)2(1)2 (cell dimensions: a = 62.0 Angstrom, b = 76.9 Angstrom, c = 87.5 Angstrom) with one molecule in the asymmetric unit. The structure was solved by Patterson search methods using Bacillus stearothermophilus PGK as a search model and was refined to a crystallographic R factor of 22.0%. Compared to the enzyme from B. stearothermophilus, horse, pig and yeast, the Thermotoga enzyme exhibits a drastically reduced interdomain angle, similar to the one reported for PGK from Trypanosoma brucei. Here we present crystallographic data of the first high-resolution structure of a PCK in largely closed conformation, complexed with the two products of the catalyzed reaction, and, at the same time, the first PGK structure from a hyperthermophilic organism.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | REFINEMENT; COMPLEX; ENZYME; phosphoglycerate kinase; Thermotoga maritima; x-ray; crystallization |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 11 May 2023 10:06 |
| Last Modified: | 11 May 2023 10:06 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50983 |
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