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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1326-34. doi: 10.1107/S1744309110037619. Epub 2010 Sep 23.

Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster.

Author information

1
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA, USA.

Abstract

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 6.1.1.2) 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-x₂₂-C-x₆-C-x₂-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.

PMID:
20944229
PMCID:
PMC2954223
DOI:
10.1107/S1744309110037619
[Indexed for MEDLINE]
Free PMC Article

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