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

Author:

Ha Lisha,Colquhoun Jennifer,Noinaj Nicholas,Das Chittaranjan,Dunman Paul M.,Flaherty Daniel P.ORCID

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.

Funder

National Institutes of Health, National Institute of Allergy and Infectious Diseases

Purdue University

Publisher

International Union of Crystallography (IUCr)

Subject

Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics

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