ArticleNucleic acids research2012
Structural basis for the substrate recognition and catalysis of peptidyl-tRNA hydrolase.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- Structural and functional analysis of peptidyl-tRNA hydrolase 2 from Candidatus Lokiarchaeum sp. GC14_75.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Association ofPathogens (Basel, Switzerland) · 2026Article
- Article
- Toxic small alarmone synthetase FaRel2 inhibits translation by pyrophosphorylating tRNAScience advances · 2024Article
- Toxic Small Alarmone Synthetase FaRel2 inhibits translation by pyrophosphorylating tRNAbioRxiv : the preprint server for biology · 2024Article
- Unveiling the Druggable Landscape of Bacterial Peptidyl tRNA Hydrolase: Insights into Structure, Function, and Therapeutic Potential.Biomolecules · 2024Review
- Peptidyl tRNA Hydrolase Is Required for Robust Prolyl-tRNA Turnover in Mycobacterium tuberculosis.mBio · 2023Article
- Natural Product Inhibition and Enzyme Kinetics Related to Phylogenetic Characterization for Bacterial Peptidyl-tRNA Hydrolase 1.Molecules (Basel, Switzerland) · 2021Article
- A unified dinucleotide alphabet describing both RNA and DNA structures.Nucleic acids research · 2020Article
- Unraveling the stereochemical and dynamic aspects of the catalytic site of bacterial peptidyl-tRNA hydrolase.RNA (New York, N.Y.) · 2017Article
- Expedited isolation of natural product peptidyl-tRNA hydrolase inhibitors from a Pth1 affinity column.AIMS molecular science · 2017Article
- A Salmonella Toxin Promotes Persister Formation through Acetylation of tRNA.Molecular cell · 2016Article
- Small Molecule Docking Supports Broad and Narrow Spectrum Potential for the Inhibition of the Novel Antibiotic Target Bacterial Pth1.Antibiotics (Basel, Switzerland) · 2016Article
- Molecular insights into the interaction of the ribosomal stalk protein with elongation factor 1α.Nucleic acids research · 2014Article
- A translation system reconstituted with human factors proves that processing of encephalomyocarditis virus proteins 2A and 2B occurs in the elongation phase of translation without eukaryotic release factors.The Journal of biological chemistry · 2014Article
- Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Å resolution shows the closed structure of the substrate-binding cleft.FEBS open bio · 2014Article
- Small molecule binding, docking, and characterization of the interaction between Pth1 and peptidyl-tRNA.International journal of molecular sciences · 2013Article
- Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptidyl-tRNA hydrolase (Pth) cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, which are produced by aborted translation, to recycle tRNA for further rounds of protein synthesis. Pth is ubiquitous in nature, and its enzymatic activity is essential for bacterial viability. We have determined the crystal structure of Escherichia coli Pth in complex with the tRNA CCA-acceptor-TΨC domain, the enzyme-binding region of the tRNA moiety of the substrate, at 2.4 Å resolution. In combination with site-directed mutagenesis studies, the structure identified the amino acid residues involved in tRNA recognition. The structure also revealed that Pth interacts with the tRNA moiety through the backbone phosphates and riboses, and no base-specific interactions were observed, except for the interaction with the highly conserved base G53. This feature enables Pth to accept the diverse sequences of the elongator-tRNAs as substrate components. Furthermore, we propose an authentic Pth:peptidyl-tRNA complex model and a detailed mechanism for the hydrolysis reaction, based on the present crystal structure and the previous studies' results.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.