Aminoacyl-tRNA synthetases.
Crystallographic studies of a number of aminoacyl-tRNA synthetases and their complexes with ATP, amino acid and cognate tRNA are leading to an increasingly detailed picture of how these sophisticated enzymes function. Within the two distinct structural classes of ten synthetases, many common features are apparent, although evolution has led to many interesting idiosyncrasies in certain enzymes. Recent advances, specifically concerning class II enzymes, have increased our knowledge of both the role of electrophiles in the mechanism of amino acid activation and cross-subunit tRNA recognition and help solve the evolutionary puzzles that have emerged from the extension of the aminoacyl-tRNA synthetase database to include Archae.
Cusack
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European Molecular Biology Laboratory, Grenoble Outstation, Institut Laue-Langevin, France.
D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology; D019143:Evolution, Molecular; D008958:Models, Molecular; D012343:RNA, Transfer / Q000737:chemistry / Q000378:metabolism; D012346:RNA, Transfer, Amino Acyl / Q000096:biosynthesis / Q000737:chemistry; D016963:Thermus thermophilus / Q000201:enzymology
D000596:Amino Acids; D012346:RNA, Transfer, Amino Acyl; D000255:Adenosine Triphosphate; D012343:RNA, Transfer; D000604:Amino Acyl-tRNA Synthetases