Structural and functional relationships between aminoacyl-tRNA synthetases.
Aminoacyl-tRNA synthetases can be divided in two groups of equal size on the basis of differences in the structure of their active sites. The core of class I synthetases is the classical nucleotide-binding domain with its characteristic Rossmann fold. In contrast, the active site of class II synthetases is built around an antiparallel beta-sheet, to which the substrates bind. This classification, which is based on structural data (amino acid sequences and tertiary structures), can be rationalized in functional terms.
Moras
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Institut de Biologie, Moléculaire et Cellulaire du CNRS, Laboratoire de Cristallographie Biologique, Strasbourg, France.
D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D005075:Biological Evolution; D011487:Protein Conformation; D012343:RNA, Transfer / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid; D013329:Structure-Activity Relationship
D012343:RNA, Transfer; D000604:Amino Acyl-tRNA Synthetases