Structural similarities in the noncatalytic domains of phenylalanyl-tRNA and biotin synthetases.
Detailed comparison between the structures of the Escherichia coli biotin synthetase/repressor protein (BirA) and the recently solved Thermus thermophilus phenylalanyl-tRNA synthetase (PheRS) reveals significant similarities outside their respective catalytic domains. These comprise a DNA-binding alpha+beta domain and an Src-homology 3 (SH3)-like domain that were observed in both enzymes. This similarity provides a novel example in which all domains of one multidomain protein appear to be constituents of the other multidomain protein and supports a concept of a common ancestor for two different synthetase families.
Safro
M
M
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Mosyak
L
L
D001665:Binding Sites; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D010652:Phenylalanine-tRNA Ligase / Q000737:chemistry*; D016415:Sequence Alignment; D013466:Sulfurtransferases / Q000737:chemistry*; D016963:Thermus thermophilus / Q000737:chemistry*; D018909:src Homology Domains
D004247:DNA; D013466:Sulfurtransferases; C057985:biotin synthetase; D010652:Phenylalanine-tRNA Ligase