In molecular biology, Domain B5 is found in phenylalanine-tRNA synthetase beta subunits. This domain has been shown to bind DNA through a winged helix-turn-helix motif.[1] Phenylalanine-tRNA synthetase may influence common cellular processes via DNA binding, in addition to its aminoacylation function.

B5 protein domain
Phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with tRNA and a phenylalanyl-adenylate analog
Identifiers
SymbolB5
PfamPF03484
InterProIPR005147
PROSITEPDOC00464
SCOP21qq3 / SCOPe / SUPFAM
TCDB5.A.4
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Function

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The beta domain, in particular, B3/B4, is required for the correct amino acid to be joined to the corresponding tRNA. Hence, the B3/B4 domain is crucial to accurate translation. Failure to do so, results in a mutated protein which improperly folds and consequently protein function is affected.[2] /B

References

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  1. ^ Dou X, Limmer S, Kreutzer R (January 2001). "DNA-binding of phenylalanyl-tRNA synthetase is accompanied by loop formation of the double-stranded DNA". J. Mol. Biol. 305 (3): 451–8. doi:10.1006/jmbi.2000.4312. PMID 11152603.
  2. ^ Roy H, Ling J, Irnov M, Ibba M (2004). "Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase". EMBO J. 23 (23): 4639–48. doi:10.1038/sj.emboj.7600474. PMC 533057. PMID 15526031.
This article incorporates text from the public domain Pfam and InterPro: IPR005147