Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan.
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.
Buddha
Madhavan R
MR
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14850, USA.
Crane
Brian R
BR
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*
C500105:4-nitro-tryptophan; D012364:RNA, Transfer, Trp; D009569:Nitric Oxide; D014364:Tryptophan; D006916:5-Hydroxytryptophan; D014369:Tryptophan-tRNA Ligase