ArticleEMBO reports2006
Coexistence of two protein folding states in the crystal structure of ribosomal protein L20.
Article in EMBO reports, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- The role of ribosomal protein networks in ribosome dynamics.Nucleic acids research · 2025Article
- Review
- Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024Article
- Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021Review
- Evolution of ribosomal protein network architectures.Scientific reports · 2021Article
- Nervous-Like Circuits in the Ribosome Facts, Hypotheses and Perspectives.International journal of molecular sciences · 2019Review
- Neuron-Like Networks Between Ribosomal Proteins Within the Ribosome.Scientific reports · 2016Article
- Interdomain Contacts Control Native State Switching of RfaH on a Dual-Funneled Landscape.PLoS computational biology · 2015Article
- The N-terminal extension of S12 influences small ribosomal subunit assembly in Escherichia coli.RNA (New York, N.Y.) · 2014Article
- Transformation: the next level of regulation.RNA biology · 2012Article
- Transformer proteins.Cell cycle (Georgetown, Tex.) · 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
- Roles of intrinsic disorder in protein-nucleic acid interactions.Molecular bioSystems · 2012Review
- Conformational analysis of the partially disordered measles virus N(TAIL)-XD complex by SDSL EPR spectroscopy.Biophysical journal · 2010Article
- SDSL-ESR-based protein structure characterization.European biophysics journal : EBJ · 2010Review
- The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 S ribosomal subunit assembly.International journal of molecular sciences · 2009Review
- Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites.Nucleic acids research · 2007Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The recent finding of intrinsically unstructured proteins defies the classical structure-function paradigm. However, owing to their flexibility, intrinsically unstructured proteins generally escape detailed structural investigations. Consequently little is known about the extent of conformational disorder and its role in biological functions. Here, we present the X-ray structure of the unbound ribosomal protein L20, the long basic amino-terminal extension of which has been previously interpreted as fully disordered in the absence of RNA. This study provides the first detailed picture of two protein folding states trapped together in a crystal and indicates that unfolding occurs in discrete regions of the whole protein, corresponding mainly to RNA-binding residues. The electrostatic destabilization of the long alpha-helix and a structural communication between the two L20 domains are reminiscent of those observed in calmodulin. The detailed comparison of the two conformations observed in the crystal provides new insights into the role of unfolded extensions in ribosomal assembly.
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