Structural highlights
Function
[SYW2_DEIRA] Catalyzes the formation of 5'adenyl-Trp and tRNA(Trp) but with 5-fold less activity than TrpRS. Increases the solubility of the nitric oxide synthase oxygenase (nos), as well as its affinity for substrate L-arginine and its nitric-oxide synthase activity. The complex between trpS2 and nos catalyzes the regioselective nitration of tryptophan at the 4-position.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan.,Buddha MR, Crane BR Nat Struct Mol Biol. 2005 Mar;12(3):274-5. Epub 2005 Feb 20. PMID:15723076[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Buddha MR, Crane BR. Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan. Nat Struct Mol Biol. 2005 Mar;12(3):274-5. Epub 2005 Feb 20. PMID:15723076 doi:10.1038/nsmb907
