Yeast aspartyl-tRNA synthetase: a structural view of the aminoacylation reaction.
The refinement of the crystal structure of a binary complex formed by yeast AspRS and tRNA(Asp) provided a detailed understanding of the recognition of tRNA by an aminoacyl-tRNA synthetase. The crystal structures of several complexes containing ATP, alone or with aspartic acid, were also determined and refined. These studies led to a complete description of the active site of the enzyme and to the elucidation of the location and interactions of the various substrates. Based on these structural results, a class II-specific pathway for the aminoacylation reaction can be proposed.
Cavarelli
J
J
Laboratoire de Biologie Structurale, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, Strasbourg, France.
Rees
B
B
Thierry
J C
JC
Moras
D
D
D000215:Acylation; D000255:Adenosine Triphosphate / Q000378:metabolism; D001226:Aspartate-tRNA Ligase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D003460:Crystallization; D018257:Helix-Loop-Helix Motifs; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D012349:RNA, Transfer, Asp / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D015003:Yeasts / Q000201:enzymology* / Q000235:genetics
D012349:RNA, Transfer, Asp; D000255:Adenosine Triphosphate; D001226:Aspartate-tRNA Ligase