Abstract
Transfer RNAs anticodon post-transcriptional modifications are responsible to the high fidelity of protein synthesis. In eubacteria, two genome-encoded transfer RNA (tRNA) species bear the same CAU sequence as the anticodons, which are differentiated by modified cytidines at the wobble positions. We have determined the structure model of the hypothetical protein. The structure unexpectedly reveals an idiosyncratic RNA helicase module fused with a GCN5-related N-acetyltransferase (GNAT) fold, which intimately cross interact. The stereo chemical quality of the protein model was checked by using in silico analysis with SWISS- MODEL, PyMol, PROCHECK, ProSA and QMEAN servers. These results may be helpful for further investigations for determining crystal structure of the hypotheitical protein and developing target molecules to inhibit Enterobacter aerogenes.
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