1YIA

Crystal structure of tryptophanyl tRNA synthetase II from Deinococcus radiodurans in complex with 5-Hydroxy tryptophan.

Summary for 1YIA

Entry DOI	10.2210/pdb1yia/pdb
Related	1YI8
Descriptor	tryptophanyl-tRNA synthetase, 5-HYDROXY-L-TRYPTOPHAN (2 entities in total)
Functional Keywords	5 hydroxy tryptophan, trna synthetase, ligase
Biological source	Deinococcus radiodurans
Total number of polymer chains	3
Total formula weight	114896.98
Authors	Buddha, M.R.,Crane, B.R. (deposition date: 2005-01-11, release date: 2005-02-22, Last modification date: 2024-02-14)
Primary citation	Buddha, M.R.,Crane, B.R. Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan. Nat.Struct.Mol.Biol., 12:274-275, 2005 Cited by PubMed 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. PubMed: 15723076 DOI: 10.1038/nsmb907 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.7 Å)

Structure validation