1yi8 | pdb_00001yi8
From Proteopedia
Crystal structure of tryptophanyl trRNA synthetase II from Deinococcus radiodurans in complex with L-Trp
| ||||||||||||
Structural highlights
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 PubMedThe 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. See AlsoReferences
Contents | ||||||||||||||||||||
This page was last modified 21:44, 28 September 2014.