Abstract:In crystal structure, the homodimeric (α2) mimi-virus Tyrosyl-tRNA Synthetases (TyrRSapm) showed significant variation in dimer orientation as compared to other solved structures of TyrRSs. Previous report showed that Bacillus stearothermophilus N-terminal TyrRS exists as dimer under native condition and unfolds through a monomeric intermediate. In our previous studies, we have reported that the C-terminal anticodon binding domain of TyrRSapm might have an indirect role in noncanonical dimer formation. To stud… Show more
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