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 RNATrp 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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Acknowledgements
We thank R.J. Parry and T. Tao for providing synthetic 4-NRP, A.M. Bilwes for help with refinement, and Cornell High Energy Synchrotron Source and the National Synchrotron Light Source for access to data collection facilities. Support from the US National Science Foundation and the US National Institutes of Health is gratefully achnowledged.
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Supplementary information
Supplementary Fig. 1
Characterization of 4-NRP incorporation into tRNA by TrpRS II. (PDF 197 kb)
Supplementary Fig. 2
Multisequence alignment of TrpRS Is and TrpRS IIs. (PDF 162 kb)
Supplementary Table 1
Diffraction data collection and refinement statistics. (PDF 81 kb)
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Buddha, M., Crane, B. Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan. Nat Struct Mol Biol 12, 274–275 (2005). https://doi.org/10.1038/nsmb907
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DOI: https://doi.org/10.1038/nsmb907
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