B5 protein domain
| B5 protein domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with tRNA and a phenylalanyl-adenylate analog | |||||||||
| Identifiers | |||||||||
| Symbol | B5 | ||||||||
| 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[edit]
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[edit]
- ^ 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.
- ^ 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.