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.
Keywords:
RNase P protein; RnpA; Staphylococcus aureus; ribonucleoprotein structure; tRNA.
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Catalytic Domain
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Cloning, Molecular
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Crystallography, X-Ray
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Gene Expression
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Genetic Vectors / chemistry
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Genetic Vectors / metabolism
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Kinetics
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Models, Molecular
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Protein Binding
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Protein Conformation, alpha-Helical
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Protein Conformation, beta-Strand
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Protein Interaction Domains and Motifs
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RNA, Bacterial / chemistry*
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RNA, Bacterial / genetics
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RNA, Bacterial / metabolism
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RNA, Transfer / chemistry*
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RNA, Transfer / genetics
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RNA, Transfer / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Ribonuclease P / chemistry*
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Ribonuclease P / genetics
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Ribonuclease P / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
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Staphylococcus aureus / chemistry*
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Staphylococcus aureus / enzymology
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Substrate Specificity
Substances
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Bacterial Proteins
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RNA, Bacterial
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Recombinant Proteins
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RNA, Transfer
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Ribonuclease P