at Google ScholarTitle data
Höcker, Birte ; Lochner, Adriane ; Seitz, Tobias ; Claren, Jörg ; Sterner, Reinhard:
High-resolution crystal structure of an artificial (βα)₈-barrel protein designed from identical half-barrels.
In: Biochemistry.
Vol. 48
(2009)
Issue 6
.
- pp. 1145-1147.
ISSN 1520-4995
DOI: https://doi.org/10.1021/bi802125b
Abstract in another language
Ample evidence suggests that the ubiquitous (betaalpha)(8)-barrel enzyme fold has evolved by the duplication and fusion of an ancestral (betaalpha)(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 (betaalpha)(8)-barrel protein HisF-C***C. The analysis of its X-ray structure at 2.1 A resolution reveals a striking similarity to wild-type HisF, helps us to understand its improved stability, and provides further insights into the evolution of (betaalpha)(8)-barrel proteins.
Further data
| Item Type: | Article in a journal |
|---|---|
| Refereed: | Yes |
| Institutions of the University: | Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Birte Höcker Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry |
| Result of work at the UBT: | No |
| DDC Subjects: | 500 Science > 540 Chemistry |
| Date Deposited: | 01 Jun 2017 07:39 |
| Last Modified: | 20 Apr 2022 12:42 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/37222 |