Abstract
Imidazole glycerol phosphate synthase (HisF) has been proposed to be the product of duplication of a gene encoding a (β/α)4-half barrel followed by fusion to encode the compmete (β/α)8-barrel. In support of this evolutionary scenario, the N- and C-terminal (β/α)4-half barrels of TrpF have been separately expressed and purified. Each assumes a stable, soluble homodimeric structure, but neither is catalytically active; when expressed together, a functional heterodimer is formed.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 5-7 |
| Number of pages | 3 |
| Journal | Nature Structural Biology |
| Volume | 8 |
| Issue number | 1 |
| DOIs | |
| State | Published - 2001 |
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Genetics