Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.
The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus, solved at 2.9 A resolution, displays (alpha beta)2 subunit organization. Unexpectedly, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains. The alpha beta heterodimer contains most of the building blocks so far identified in the class II synthetases. The presence of an RNA-binding domain, similar to that of the U1A spliceosomal protein, in the beta-subunit is indicative of structural relationships among different families of RNA-binding proteins. The structure suggests a plausible catalytic mechanism which explains why the primary site of tRNA aminoacylation is different from that of the other class II enzymes.
Mosyak
L
L
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Reshetnikova
L
L
Goldgur
Y
Y
Delarue
M
M
Safro
M G
MG
D000255:Adenosine Triphosphate / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology; D001426:Bacterial Proteins / Q000648:ultrastructure; D001483:Base Sequence; D001665:Binding Sites; D005075:Biological Evolution; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010652:Phenylalanine-tRNA Ligase / Q000648:ultrastructure*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D016963:Thermus thermophilus / Q000201:enzymology*
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D000255:Adenosine Triphosphate; D010652:Phenylalanine-tRNA Ligase