Báo cáo khoa học: Flexibility and communication within the structure of the Mycobacterium smegmatis methionyl-tRNA synthetase Henrik Ingvarsson and Torsten Unge
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Two structures of monomeric methionyl-tRNA synthetase, fromMycobac-terium smegmatis, in complex with the ligands methionine⁄adenosine and methionine, were analyzed by X-ray crystallography at 2.3 A˚ and at 2.8 A˚ , respectively. The structures demonstrated the flexibility of the multidomain enzyme. A new conformation of the structure was identified in which the connective peptide domain bound more closely to the catalytic domain than described previously.
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