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B5 protein domain
| Field | Value |
|---|---|
| Symbol | B5 |
| Name | B5 protein domain |
| image | PDB 2iy5 EBI.jpg |
| caption | Phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with tRNA and a phenylalanyl-adenylate analog |
| Pfam | PF03484 |
| InterPro | IPR005147 |
| PROSITE | PDOC00464 |
| SCOP | 1qq3 |
| 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. 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. /B
References
References
- (January 2001). "DNA-binding of phenylalanyl-tRNA synthetase is accompanied by loop formation of the double-stranded DNA". J. Mol. Biol..
- (2004). "Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase.". EMBO J.
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