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- W2891434028 abstract "Staphylococcus aureus ribonuclease-P-protein subunit (RnpA) is a promising antimicrobial target that is a key protein component for two essential cellular processes, RNA degradation and transfer-RNA (tRNA) maturation. The first crystal structure of RnpA from the pathogenic bacterial species, S. aureus, is reported at 2.0 Å resolution. The structure presented maintains key similarities with previously reported RnpA structures from bacteria and archaea, including the highly conserved RNR-box region and aromatic residues in the precursor-tRNA 5'-leader-binding domain. This structure will be instrumental in the pursuit of structure-based designed inhibitors targeting RnpA-mediated RNA processing as a novel therapeutic approach for treating S. aureus infections." @default.
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- W2891434028 date "2018-09-19" @default.
- W2891434028 modified "2023-10-17" @default.
- W2891434028 title "Crystal structure of the ribonuclease-P-protein subunit from <i>Staphylococcus aureus</i>" @default.
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- W2891434028 doi "https://doi.org/10.1107/s2053230x18011512" @default.
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