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Crystal structure of the ribonuclease‐P‐protein subunit from Staphylococcus aureus
Author(s) -
Ha Lisha,
Colquhoun Jennifer,
Noinaj Nicholas,
Das Chittaranjan,
Dunman Paul M.,
Flaherty Daniel P.
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18011512
Subject(s) - ribonuclease , transfer rna , staphylococcus aureus , rna , protein subunit , archaea , bacteria , biology , microbiology and biotechnology , chemistry , biochemistry , computational biology , genetics , gene
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.