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Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus.

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.

SUBMITTER: Ha L

PROVIDER: S-EPMC6168776 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus.

Ha Lisha L Colquhoun Jennifer J Noinaj Nicholas N Das Chittaranjan C Dunman Paul M PM Flaherty Daniel P DP

Acta crystallographica. Section F, Structural biology communications 20180919 Pt 10

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 regio ...[more]

PMID: 30279314

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