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- W2043009066 abstract "The C-terminal domain (residues 320–419) of tyrosyl-tRNA synthetase (TyrRS) from Bacillus stearothermophilus is disordered in the crystal structure and involved in the binding of the anticodon arm of tRNATyr. The sequences of 11 TyrRSs of prokaryotic or mitochondrial origins were aligned and the alignment showed the existence of conserved residues in the sequences of the C-terminal domains. A consensus could be deduced from the application of five programs of secondary structure prediction to the 11 sequences of the query set. These results suggested that the sequences of the C-terminal domains determined a precise and conserved secondary structure. They predicted that the C-terminal domain would have a mixed fold (α/β or α+β), with the α-helices in the first half of the sequence and the β-strands mainly in its second half. Several programs of fold recognition from sequence alone, by threading onto known structures, were applied but none of them identified a type of fold that would be common to the different sequences of the query set. Therefore, the fold of the C-terminal, anticodon binding domain might be novel." @default.
- W2043009066 created "2016-06-24" @default.
- W2043009066 creator A5011884737 @default.
- W2043009066 creator A5027912576 @default.
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- W2043009066 date "1999-03-01" @default.
- W2043009066 modified "2023-09-25" @default.
- W2043009066 title "Disordered C-terminal domain of tyrosyl-tRNA synthetase: Secondary structure prediction" @default.
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- W2043009066 doi "https://doi.org/10.1016/s0300-9084(99)80057-1" @default.
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