Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan |
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Authors: | Buddha Madhavan R Crane Brian R |
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Institution: | Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14850, USA. |
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Abstract: | The most divergent of two tryptophanyl tRNA synthetases (TrpRS II) found in Deinococcus radiodurans interacts with a nitric oxide synthase protein that produces 4-nitro-tryptophan (4-NRP). TrpRS II efficiently charges transfer RNA(Trp) with 4-NRP and 5-hydroxy-tryptophan (5-HRP). The crystal structures of TrpRS II bound to tryptophan and 5-HRP reveal residue substitutions that accommodate modified indoles. A class of auxiliary bacterial TrpRSs conserve this capacity to charge tRNA with nonstandard amino acids. |
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