Crystal structure of the ribonuclease‐P‐protein subunit from Staphylococcus aureus. Issue 10 (3rd October 2018)

• Record Type: Journal Article
• Authors: Ha, Lisha; Colquhoun, Jennifer; Noinaj, Nicholas; Das, Chittaranjan; Dunman, Paul M.; Flaherty, Daniel P.
• Is Part Of: Acta crystallographica. Volume 74:Issue 10(2018:Oct.)
• Page Start: 632
• Page End: 637
• Publication Date: 2018-10-03
• Subjects: ribonucleoprotein structure -- RnpA -- RNase P protein -- Staphylococcus aureus -- tRNA; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X18011512
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : Staphylococcus aureus ribonuclease‐P‐protein subunit (RnpA) is a promising antimicrobial target. The crystal structure of RnpA at 2.0 Å resolution shows key similarities with RnpA structures from bacteria and archaea and will be instrumental in designing inhibitors targeting RnpA‐mediated RNA processing. 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.