4j9j

Publication Abstract from PubMed

It has been postulated that the ubiquitous (betaalpha)8-barrel enzyme fold has evolved by duplication and fusion of an ancestral (betaalpha)4-half-barrel. We have previously reconstructed this process in the laboratory by fusing two copies of the C-terminal half-barrel HisF-C of imidazole glycerol phosphate synthase (HisF). The resulting construct HisF-CC was stepwise stabilized to Sym1 and Sym2, which are extremely robust but catalytically inert proteins. Here, we report on the generation of a circular permutant of Sym2 and the establishment of a sugar isomerization reaction on its scaffold. Our results demonstrate that duplication and mutagenesis of (betaalpha)4-half-barrels can readily lead to a stable and catalytically active (betaalpha)8-barrel enzyme.

Establishing catalytic activity on an artificial (betaalpha)-barrel protein designed from identical half-barrels.,Sperl JM, Rohweder B, Rajendran C, Sterner R FEBS Lett. 2013 Jun 24. pii: S0014-5793(13)00469-9. doi:, 10.1016/j.febslet.2013.06.022. PMID:23806364^[1]

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