ArticleProtein science : a publication of the Protein Society2008
Solution structure of ribosomal protein L40E, a unique C4 zinc finger protein encoded by archaeon Sulfolobus solfataricus.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Ribosome remodeling drives translation adaptation during viral infection and cellular stress.Molecular cell · 2026Article
- A molecular switch controls assembly of bacterial focal adhesions.Science advances · 2024Article
- Solution NMR structure of zinc finger 4 and 5 from human INSM1, an essential regulator of neuroendocrine differentiation.Proteins · 2017Article
- Disordered proteinaceous machines.Chemical reviews · 2014Review
- A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome.Cellular and molecular life sciences : CMLS · 2014Article
- Yeast ribosomal protein L40 assembles late into precursor 60 S ribosomes and is required for their cytoplasmic maturation.The Journal of biological chemistry · 2012Article
- Cryo-EM structure of the archaeal 50S ribosomal subunit in complex with initiation factor 6 and implications for ribosome evolution.Journal of molecular biology · 2012Article
- Molecular signatures of ribosomal evolution.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The ribosomal protein L40E from archaeon Sulfolobus solfataricus is a component of the 50S ribosomal subunit. L40E is a 56-residue, highly basic protein that contains a C4 zinc finger motif, CRKC_X(10)_CRRC. Homologs are found in both archaea and eukaryotes but are not present in bacteria. Eukaryotic genomes encode L40E as a ubiquitin-fusion protein. L40E was absent from the crystal structure of euryarchaeota 50S ribosomal subunit. Here we report the three-dimensional solution structure of L40E by NMR spectroscopy. The structure of L40E is a three-stranded beta-sheet with a simple beta2beta1beta3 topology. There are two unique characteristics revealed by the structure. First, a large and ordered beta2-beta3 loop twists to pack across the one side of the protein. L40E contains a buried polar cluster comprising Lys19, Lys20, Cys22, Asn29, and Cys36. Second, the surface of L40E is almost entirely positively charged. Ten conserved basic residues are positioned on the two sides of the surface. It is likely that binding of zinc is essential in stabilizing the tertiary structure of L40E to act as a scaffold to create a broad positively charged surface for RNA and/or protein recognition.
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Registered trials
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