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PROSITE documentation PDOC51483 [for PROSITE entry PS51483]

B5 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. It is a heterodimeric class II enzyme of the (αβ)2 type. The αβ heterodimer of Thermus thermophilus is composed of ten structural domains: two of them A1-A2 belong to the α subunit and eight B1-B8 to the β subunit. The B5 domain is formed by three α-helices and three antiparallel β-strands and comprises a surface-exposed "winged" helix-turn-helix (HTH) motif (see <PDB:1PYS>) [1,2,3]. The B5 domain has been shown to bind DNA [4].

The profile we developed covers the entire B5 domain.

Last update:

March 2010 / First entry.

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Technical section

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

B5, PS51483; B5 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

2AuthorsRodova 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

3AuthorsMoor 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

4AuthorsDou X. Limmer S. Kreutzer R.
TitleDNA-binding of phenylalanyl-tRNA synthetase is accompanied by loop formation of the double-stranded DNA.
SourceJ. Mol. Biol. 305:451-458(2001).
PubMed ID11152603
DOI10.1006/jmbi.2000.4312



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