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Structure and Activity of an Aminoacyl-tRNA Synthetase that Charges tRNA with Nitro-Tryptophan

Journal Article · · Nature Structural and Molecular Biology
DOI:https://doi.org/10.1038/nsmb907· OSTI ID:959844
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.
Research Organization:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Organization:
Doe - Office Of Science
DOE Contract Number:
AC02-98CH10886
OSTI ID:
959844
Report Number(s):
BNL--82830-2009-JA
Journal Information:
Nature Structural and Molecular Biology, Journal Name: Nature Structural and Molecular Biology Journal Issue: 3 Vol. 12
Country of Publication:
United States
Language:
English

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