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) |
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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