Substrate selection by aminoacyl-tRNA synthetases.
The integration of genetic and biochemical approaches to study the crystal structure of the glutaminyl-tRNA synthetase (GlnRS):tRNA(Gln):ATP complex has elucidated the mechanism by which GlnRS selects its cognate tRNA for aminoacylation. Three principal types of interaction have been identified: interaction with specific bases in the cognate tRNA, rejection of non-cognate tRNAs, and activation of the active site upon cognate tRNA binding. The recent solving of the crystal structure of tryptophanyl-tRNA synthetase (TrpRS) has allowed comparable studies to be initiated in an aminoacyl-tRNA synthetase which, unlike GlnRS, does not require tRNA binding prior to amino acid activation.
Ibba
M
M
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511, USA.
Thomann
H U
HU
Hong
K W
KW
Sherman
J M
JM
Weygand-Durasevic
I
I
Sever
S
S
Stange-Thomann
N
N
Praetorius
M
M
Söll
D
D
D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D001411:Geobacillus stearothermophilus / Q000201:enzymology / Q000235:genetics; D005975:Glutamate-tRNA Ligase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D009154:Mutation; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D012351:RNA, Transfer, Gln / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D014369:Tryptophan-tRNA Ligase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D012351:RNA, Transfer, Gln; D000604:Amino Acyl-tRNA Synthetases; D005975:Glutamate-tRNA Ligase; D014369:Tryptophan-tRNA Ligase