Home  |  Contact
PROSITE documentation PDOC51447 [for PROSITE entry PS51447]

Ferredoxin-fold anticodon binding (FDX-ACB) domain profile





Description

Aminoacyl-tRNA synthetases (aaRSs) play a crucial role in the translation of the genetic code by means of covalent attachment of amino acids to their cognate tRNAs. Phenylalanine--tRNA synthetase (PheRS) is known to be among the most complex enzymes of the aaRS family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double split α+β motif having no insertions. The FDX-ACB domain displays a typical RNA recognition fold (RRM) (see <PDOC00030>) formed by the four-stranded antiparallel β sheet, with two helices packed against it (see <PDB:3CMQ>) [1,2,3,4,5].

The profile we developed covers the entire FDX-ACB domain.

Last update:

April 2009 / First entry.

-------------------------------------------------------------------------------

Technical section

PROSITE method (with tools and information) covered by this documentation:

FDX_ACB, PS51447; Ferredoxin-fold anticodon binding (FDX-ACB) domain profile  (MATRIX)


References

1AuthorsMosyak L. Reshetnikova L. Goldgur Y. Delarue M. Safro M.G.
TitleStructure of phenylalanyl-tRNA synthetase from Thermus thermophilus.
SourceNat. Struct. Biol. 2:537-547(1995).
PubMed ID7664121

2AuthorsGoldgur Y. Mosyak L. Reshetnikova L. Ankilova V. Lavrik O. Khodyreva S. Safro M.
TitleThe crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe.
SourceStructure 5:59-68(1997).
PubMed ID9016717

3AuthorsRodova M. Ankilova V. Safro M.G.
TitleHuman phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells.
SourceBiochem. Biophys. Res. Commun. 255:765-773(1999).
PubMed ID10049785
DOI10.1006/bbrc.1999.0141

4AuthorsMoor N. Lavrik O. Favre A. Safro M.
TitleProkaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end.
SourceBiochemistry 42:10697-10708(2003).
PubMed ID12962494
DOI10.1021/bi034732q

5AuthorsKlipcan L. Levin I. Kessler N. Moor N. Finarov I. Safro M.
TitleThe tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase.
SourceStructure 16:1095-1104(2008).
PubMed ID18611382
DOI10.1016/j.str.2008.03.020



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)