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Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2010 Oct 01; Vol. 66 (Pt 10), pp. 1326-34. Date of Electronic Publication: 2010 Sep 23. - Publication Year :
- 2010
-
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.
- Subjects :
- Amino Acid Sequence
Animals
Conserved Sequence
Crystallography, X-Ray
Humans
Ligands
Models, Molecular
Molecular Sequence Data
Protein Structure, Quaternary
Protein Structure, Tertiary
Sequence Alignment
Iron-Sulfur Proteins chemistry
Thermotoga maritima enzymology
Tryptophan-tRNA Ligase chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 66
- Issue :
- Pt 10
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 20944229
- Full Text :
- https://doi.org/10.1107/S1744309110037619