National Center for
2G36: Crystal Structure Of Tryptophanyl-trna Synthetase (ec 18.104.22.168) (tryptophan-trna Ligase)(trprs) (tm0492) From Thermotoga Maritima At 2.50 A Resolution
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (2010) 66 p.1326-1334
A novel aminoacyl-tRNA synthetase that contains an iron-sulfur cluster in the tRNA anticodon-binding region and efficiently charges tRNA with tryptophan has been found in Thermotoga maritima. The crystal structure of TmTrpRS (tryptophanyl-tRNA synthetase; TrpRS; EC 22.214.171.124) reveals an iron-sulfur [4Fe-4S] cluster bound to the tRNA anticodon-binding (TAB) domain and an L-tryptophan ligand in the active site. None of the other T. maritima aminoacyl-tRNA synthetases (AARSs) contain this [4Fe-4S] cluster-binding motif (C-x(2)(2)-C-x(6)-C-x(2)-C). It is speculated that the iron-sulfur cluster contributes to the stability of TmTrpRS and could play a role in the recognition of the anticodon.