Crystal structure of histidyl‐tRNA synthetase from Escherichia coli complexed with histidyl‐adenylate

The crystal structure at 2.6 A of the histidyl‐tRNA synthetase from Escherichia coli complexed with histidyl‐adenylate has been determined. The enzyme is a homodimer with a molecular weight of 94 kDa and belongs to the class II of aminoacyl‐tRNA synthetases (aaRS). The asymmetric unit is composed of...

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Bibliographic Details
Published in:	The EMBO journal Vol. 14; no. 17; pp. 4143 - 4155
Main Authors:	Arnez, J. G., Harris, D. C., Mitschler, A., Rees, B., Francklyn, C. S., Moras, D.
Format:	Journal Article
Language:	English
Published:	England 01-09-1995
Subjects:	Adenosine - analogs & derivatives Adenosine - metabolism Amino Acid Sequence Binding Sites Biochemistry, Molecular Biology Crystallography, X-Ray - methods Escherichia coli Escherichia coli - enzymology Histidine - analogs & derivatives Histidine - metabolism Histidine-tRNA Ligase - chemistry Histidine-tRNA Ligase - isolation & purification Histidine-tRNA Ligase - metabolism Life Sciences Macromolecular Substances Models, Molecular Molecular Sequence Data Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism tRNA
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