Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan (original) (raw)
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- Published: 20 February 2005
Nature Structural & Molecular Biology volume 12, pages 274–275 (2005)Cite this article
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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 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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Figure 1: Comparison of tryptophan and 5-HRP recognition by drTrpRS II and bsTrpRS (PDB entry 1MB2).
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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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- Department of Chemistry and Chemical Biology, Cornell University, Ithaca, 14850, New York, USA
Madhavan R Buddha & Brian R Crane
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- Madhavan R Buddha
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Correspondence toBrian R Crane.
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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
- Received: 13 December 2004
- Accepted: 01 February 2005
- Published: 20 February 2005
- Issue Date: 01 March 2005
- DOI: https://doi.org/10.1038/nsmb907