Structural highlights
Function
[RNPA_STAAU] RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Publication Abstract from PubMed
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 A 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.
Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus.,Ha L, Colquhoun J, Noinaj N, Das C, Dunman PM, Flaherty DP Acta Crystallogr F Struct Biol Commun. 2018 Oct 1;74(Pt 10):632-637. doi:, 10.1107/S2053230X18011512. Epub 2018 Sep 19. PMID:30279314[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ha L, Colquhoun J, Noinaj N, Das C, Dunman PM, Flaherty DP. Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus. Acta Crystallogr F Struct Biol Commun. 2018 Oct 1;74(Pt 10):632-637. doi:, 10.1107/S2053230X18011512. Epub 2018 Sep 19. PMID:30279314 doi:http://dx.doi.org/10.1107/S2053230X18011512
