ArticleRNA (New York, N.Y.)2002
Detailed analysis of RNA-protein interactions within the bacterial ribosomal protein L5/5S rRNA complex.
Article in RNA (New York, N.Y.), 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Crystal Structures of Cyanine Fluorophores Stacked onto the End of Double-Stranded RNA.Biophysical journal · 2017Article
- Protein L5 is crucial for in vivo assembly of the bacterial 50S ribosomal subunit central protuberance.Nucleic acids research · 2012Article
- Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135.BMC research notes · 2010Article
- Identification of proteins from prunus persica that interact with peach latent mosaic viroid.Journal of virology · 2009Article
- Comprehensive analysis of phosphorylated proteins of Escherichia coli ribosomes.Journal of proteome research · 2009Article
- Article
- Functional features of the C-terminal region of yeast ribosomal protein L5.Molecular genetics and genomics : MGG · 2008Article
- Analyzing the flexibility of RNA structures by constraint counting.Biophysical journal · 2008Article
- Article
- Changes in the conformation of 5S rRNA cause alterations in principal functions of the ribosomal nanomachine.Nucleic acids research · 2007Article
- Long-residency hydration, cation binding, and dynamics of loop E/helix IV rRNA-L25 protein complex.Biophysical journal · 2004Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The crystal structure of ribosomal protein L5 from Thermus thermophilus complexed with a 34-nt fragment comprising helix III and loop C of Escherichia coli 5S rRNA has been determined at 2.5 A resolution. The protein specifically interacts with the bulged nucleotides at the top of loop C of 5S rRNA. The rRNA and protein contact surfaces are strongly stabilized by intramolecular interactions. Charged and polar atoms forming the network of conserved intermolecular hydrogen bonds are located in two narrow planar parallel layers belonging to the protein and rRNA, respectively. The regions, including these atoms conserved in Bacteria and Archaea, can be considered an RNA-protein recognition module. Comparison of the T. thermophilus L5 structure in the RNA-bound form with the isolated Bacillus stearothermophilus L5 structure shows that the RNA-recognition module on the protein surface does not undergo significant changes upon RNA binding. In the crystal of the complex, the protein interacts with another RNA molecule in the asymmetric unit through the beta-sheet concave surface. This protein/RNA interface simulates the interaction of L5 with 23S rRNA observed in the Haloarcula marismortui 50S ribosomal subunit.
Indexed as
Identifiers
12515387PMC1370360W2138173049What OpenQuestion holds
Registered trials
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.