ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- The crystal structures of apo and tryptophan-bound tryptophanyl-tRNA synthetase from Neisseria gonorrhoeae.Acta crystallographica. Section F, Structural biology communications · 2025Article
- An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening.Nucleic acids research · 2023Article
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- Bioinformatic Analysis Reveals Archaeal tRNALife (Basel, Switzerland) · 2017Article
- The Relationship between Environmental Dioxygen and Iron-Sulfur Proteins Explored at the Genome Level.PloS one · 2017Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Structural principles for computational and de novo design of 4Fe-4S metalloproteins.Biochimica et biophysica acta · 2016Review
- The widespread role of non-enzymatic reactions in cellular metabolism.Current opinion in biotechnology · 2015Review
- A role for [Fe4S4] clusters in tRNA recognition--a theoretical study.Nucleic acids research · 2014Article
- Emergence and evolution.Topics in current chemistry · 2014Review
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Authors and funding
44 authors at 7 institutions in 1 country.
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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.
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