Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan

• Published in: Nature structural & molecular biology Vol. 12; no. 3; pp. 274 - 275
• Main Authors: Crane, Brian R, Buddha, Madhavan R
• Format: Journal Article
• Language: English
• Published: United States Nature Publishing Group 01.03.2005
• Subjects: 5-Hydroxytryptophan - metabolism; Amino acids; Aminoacyl-tRNA synthetases; Catalysis; Crystallography; Deinococcus - enzymology; Deinococcus radiodurans; Indoles; Molecular Structure; Nitric oxide; Nitric Oxide - metabolism; Physiological aspects; Proteins; RNA, Transfer, Trp - metabolism; Structure; Substrate Specificity; Transfer RNA; Tryptophan; Tryptophan - analogs & derivatives; Tryptophan - metabolism; Tryptophan-tRNA Ligase - chemistry; Tryptophan-tRNA Ligase - metabolism; United States
• ISSN: 1545-9993; 1545-9985
• DOI: 10.1038/nsmb907

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.