ArticleProtein science : a publication of the Protein Society2004
Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 9 citations in OpenAlex.
- Structures of tmRNA and SmpB as they transit through the ribosome.Nature communications · 2021Article
- Structural modeling and functional analysis of the essential ribosomal processing protease Prp from Staphylococcus aureus.Molecular microbiology · 2017Article
- Specific N-terminal cleavage of ribosomal protein L27 in Staphylococcus aureus and related bacteria.Molecular microbiology · 2015Article
- The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase.Nucleic acids research · 2013Article
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9 authors at 2 institutions in 1 country.
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Abstract
Ribosomal protein L27 is located near the peptidyltransferase center at the interface of ribosomal subunits, and is important for ribosomal assembly and function. We report the crystal structure of ribosomal protein L27 from Thermus thermophilus HB8, which was determined by the multiwavelength anomalous dispersion method and refined to an R-factor of 19.7% (R(free) = 23.6%) at 2.8 A resolution. The overall fold is an all beta-sheet hybrid. It consists of two sets of four-stranded beta-sheets formed around a well-defined hydrophobic core, with a highly positive charge on the protein surface. The structure of ribosomal protein L27 from T. thermophilus HB8 in the RNA-free form is investigated, and its functional roles in the ribosomal subunit are discussed.
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