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

Journal Article · Sat Jan 01 00:00:00 EST 2005 · Nature Structural and Molecular Biology

DOI:https://doi.org/10.1038/nsmb907· OSTI ID:959844

Buddha, M; Crane, B

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 Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: DE-AC02-98CH10886
• OSTI ID: 959844
• Report Number(s): BNL-82830-2009-JA; TRN: US201016%%988
• Journal Information: Nature Structural and Molecular Biology, Vol. 12, Issue 3
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
AMINO ACIDS
CAPACITY
CRYSTAL STRUCTURE
INDOLES
LIGASES
NITRIC OXIDE
PROTEINS
RESIDUES
TRYPTOPHAN
national synchrotron light source