Abstract
The atomic structures of two proteins in the histidine biosynthesis pathway consist of beta/alpha barrels with a twofold repeat pattern. It is likely that these proteins evolved by twofold gene duplication and gene fusion from a common half-barrel ancestor. These ancestral domains are not visible as independent domains in the extant proteins but can be inferred from a combination of sequence and structural analysis. The detection of subdomain structures may be useful in efforts to search genome sequences for functionally and structurally related proteins.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Aldose-Ketose Isomerases / chemistry*
-
Aldose-Ketose Isomerases / genetics
-
Aldose-Ketose Isomerases / metabolism
-
Amino Acid Motifs
-
Amino Acid Sequence
-
Aminohydrolases / chemistry*
-
Aminohydrolases / genetics
-
Aminohydrolases / metabolism
-
Binding Sites
-
Catalysis
-
Crystallography, X-Ray
-
Evolution, Molecular*
-
Gene Duplication*
-
Histidine / biosynthesis
-
Models, Molecular
-
Molecular Sequence Data
-
Protein Folding
-
Protein Structure, Tertiary*
-
Recombination, Genetic*
-
Sequence Alignment
-
Thermotoga maritima / enzymology
Substances
-
Histidine
-
imidazole glycerol phosphate synthase
-
Aminohydrolases
-
Aldose-Ketose Isomerases
-
Phosphoribosyl-5-amino-1-phosphoribosyl-4-imidazolecarboxiamide isomerase