B5 protein domain
|This article is an orphan, as no other articles link to it. Please introduce links to this page from ; try the Find links tool for suggestions. (July 2012)|
|B5 protein domain|
Phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with tRNA and a phenylalanyl-adenylate analog
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. Phenylalanine-tRNA synthetase may influence common cellular processes via DNA binding, in addition to its aminoacylation function.
The beta domain, in particular, B5, is required for the correct amino acid to be joined to the corresponding tRNA. Hence, the B5 domain is crucial to accurate translation. Failure to do so, results in a mutated protein which improperly folds and consequently protein function is affected.
- 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): 451â8. 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.