Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase

The structure of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNA2Gln and ATP refined at 2.5-A resolution reveals structural details of the catalytic center and allows description of the specific roles of individual amino acid residues in substrate binding and catalysis. The reactive...

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Veröffentlicht in:	Biochemistry (Easton) 1993-08, Vol.32 (34), p.8758-8771
Hauptverfasser:	Perona, John J, Rould, Mark A, Steitz, Thomas A
Format:	Artikel
Sprache:	eng
Schlagworte:	Acylation Adenosine Monophosphate - metabolism Adenosine Triphosphate - metabolism Amino Acid Sequence Amino Acyl-tRNA Synthetases - metabolism Analytical, structural and metabolic biochemistry Binding Sites Biological and medical sciences Catalysis Enzymes and enzyme inhibitors Escherichia coli Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Glutamine - metabolism Ligases Magnesium - metabolism Molecular Sequence Data Protein Conformation RNA, Transfer, Glu - chemistry RNA, Transfer, Glu - metabolism
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