B5 protein domain

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B5 protein domain
PDB 2iy5 EBI.jpg
Phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with tRNA and a phenylalanyl-adenylate analog
Identifiers
SymbolB5
Pfam PF03484
InterPro IPR005147
PROSITE PDOC00464
SCOP2 1qq3 / SCOPe / SUPFAM
TCDB 5.A.4

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.

Function

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

Related Research Articles

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Phenylalanine—tRNA ligase

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FARSB

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Phenylalanyl-tRNA synthetase alpha chain is an enzyme that in humans is encoded by the FARSA gene.

FARS2

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FPG IleRS zinc finger

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B3/B4 tRNA-binding domain

The B3/B4 domain, is found in tRNA synthetase beta subunits, as well as in some non-tRNA synthetase proteins.

Solenoid protein domain

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References

  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