title: Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan.
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 RNA(Trp) 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.
authors.affiliation: Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14850, USA.
authors.forename: Madhavan R
authors.initials: MR
authors.lastname: Buddha
authors.forename: Brian R
authors.initials: BR
authors.lastname: Crane
mesh_terms: D006916:5-Hydroxytryptophan / Q000378:metabolism; D002384:Catalysis; D003461:Crystallography; D034301:Deinococcus / Q000201:enzymology; D015394:Molecular Structure; D009569:Nitric Oxide / Q000378:metabolism; D012364:RNA, Transfer, Trp / Q000378:metabolism*; D013379:Substrate Specificity; D014364:Tryptophan / Q000031:analogs & derivatives* / Q000378:metabolism*; D014369:Tryptophan-tRNA Ligase / Q000737:chemistry* / Q000378:metabolism*
chemical_list: C500105:4-nitro-tryptophan; D012364:RNA, Transfer, Trp; D009569:Nitric Oxide; D014364:Tryptophan; D006916:5-Hydroxytryptophan; D014369:Tryptophan-tRNA Ligase