Buddha Madhavan R, Crane Brian R
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14850, USA.
Nat Struct Mol Biol. 2005 Mar;12(3):274-5. doi: 10.1038/nsmb907. Epub 2005 Feb 20.
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.
在耐辐射球菌中发现的两种色氨酰-tRNA合成酶（TrpRS II）中，差异最大的一种与一种产生4-硝基色氨酸（4-NRP）的一氧化氮合酶蛋白相互作用。TrpRS II能有效地将4-NRP和5-羟色氨酸（5-HRP）装载到转运RNA（Trp）上。与色氨酸和5-HRP结合的TrpRS II的晶体结构揭示了适应修饰吲哚的残基取代。一类辅助性细菌TrpRS保留了用非标准氨基酸装载tRNA的这种能力。
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