6D1R
Structure of Staphylococcus aureus RNase P protein at 2.0 angstrom
Summary for 6D1R
| Entry DOI | 10.2210/pdb6d1r/pdb |
| Descriptor | Ribonuclease P protein component (2 entities in total) |
| Functional Keywords | rnase, p protein, trna processing, rna metabolism, rna binding protein |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 13829.41 |
| Authors | Ha, L.,Colquhoun, J.,Noinaj, N.,Das, C.,Dunman, P.,Flaherty, D.P. (deposition date: 2018-04-12, release date: 2018-09-26, Last modification date: 2024-03-13) |
| Primary citation | Ha, L.,Colquhoun, J.,Noinaj, N.,Das, C.,Dunman, P.M.,Flaherty, D.P. Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus. Acta Crystallogr F Struct Biol Commun, 74:632-637, 2018 Cited by PubMed 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. PubMed: 30279314DOI: 10.1107/S2053230X18011512 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.995 Å) |
Structure validation
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