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High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels

Title data

Höcker, Birte ; Lochner, Adriane ; Seitz, Tobias ; Claren, Jörg ; Sterner, Reinhard:
High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels.
In: Biochemistry. Vol. 48 (17 February 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: 01 Jun 2017 10:05
URI: https://eref.uni-bayreuth.de/id/eprint/37222