2w6r

Publication Abstract from PubMed

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.

High-Resolution Crystal Structure of an Artificial (betaalpha)(8)-Barrel Protein Designed from Identical Half-Barrels (dagger) (double dagger).,Hocker B, Lochner A, Seitz T, Claren J, Sterner R Biochemistry. 2009 Jan 23. PMID:19166324^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.