Cavarelli J, Rees B, Thierry J C, Moras D
Laboratoire de Biologie Structurale, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, Strasbourg, France.
Biochimie. 1993;75(12):1117-23. doi: 10.1016/0300-9084(93)90011-g.
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.
酵母天冬酰胺-tRNA合成酶（AspRS）与天冬氨酸tRNA（tRNA(Asp)）形成的二元复合物晶体结构的优化，使得人们对氨酰-tRNA合成酶识别tRNA有了详细的了解。还测定并优化了几种单独含有ATP或与天冬氨酸结合的复合物的晶体结构。这些研究对该酶的活性位点进行了完整描述，并阐明了各种底物的位置和相互作用。基于这些结构结果，可以提出II类氨酰化反应的特定途径。
