PROSITE documentation PDOC51483B5 domain profile
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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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Mosyak L. Reshetnikova L. Goldgur Y. Delarue M. Safro M.G. |
| Title | Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus. | |
| Source | Nat. Struct. Biol. 2:537-547(1995). | |
| PubMed ID | 7664121 |
| 2 | Authors | Rodova M. Ankilova V. Safro M.G. |
| Title | Human 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. | |
| Source | Biochem. Biophys. Res. Commun. 255:765-773(1999). | |
| PubMed ID | 10049785 | |
| DOI | 10.1006/bbrc.1999.0141 |
| 3 | Authors | Moor N. Lavrik O. Favre A. Safro M. |
| Title | Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end. | |
| Source | Biochemistry 42:10697-10708(2003). | |
| PubMed ID | 12962494 | |
| DOI | 10.1021/bi034732q |
| 4 | Authors | Dou X. Limmer S. Kreutzer R. |
| Title | DNA-binding of phenylalanyl-tRNA synthetase is accompanied by loop formation of the double-stranded DNA. | |
| Source | J. Mol. Biol. 305:451-458(2001). | |
| PubMed ID | 11152603 | |
| DOI | 10.1006/jmbi.2000.4312 |
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