Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan
- 20 February 2005
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 12 (3), 274-275
- https://doi.org/10.1038/nsmb907
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.Keywords
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