Hoecker, Birte and Lochner, Adriane and Seitz, Tobias and Claren, Joerg and Sterner, Reinhard (2009) High-Resolution Crystal Structure of an Artificial (beta alpha)(8)-Barrel Protein Designed from Identical Half-Barrels. BIOCHEMISTRY, 48 (6). pp. 1145-1147. ISSN 0006-2960,
Full text not available from this repository. (Request a copy)Abstract
Ample evidence suggests that the ubiquitous (beta alpha)(8)-barrel enzyme fold has evolved by the duplication and fusion of an ancestral (beta alpha)(4)-half-barrel. To reconstruct this process in the laboratory with a model protein, we earlier fused two copies of the C-terminal half-barrel HisF-C of imidazole glycerol phosphate synthase, (HisF) and stepwise stabilized the resulting HisF-CC construct. We now further increased its stability and Solubility by introducing two additional amino acid exchanges, which allowed us to crystallize the resulting artificial (beta alpha)(8)-barrel protein HisF-C***C. The analysis of its X-ray structure at 2.1 angstrom resolution reveals a striking similarity to wildtype HisF, helps us to understand its improved stability, and provides further insights into the evolution of (beta alpha)(8)-barrel proteins.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | EVOLUTION; COMBINATION; FRAGMENTS; ENZYMES; FOLD; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 05 Oct 2020 09:43 |
| Last Modified: | 05 Oct 2020 09:43 |
| URI: | https://pred.uni-regensburg.de/id/eprint/29468 |
Actions (login required)
 |
View Item |
