ArticleBiophysical journal2010
Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR Relaxation.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 76 citations in OpenAlex.
- Phosphorylation of P-stalk proteins defines the ribosomal state for interaction with auxiliary protein factors.EMBO reports · 2024Article
- Archaea/eukaryote-specific ribosomal proteins - guardians of a complex structure.Computational and structural biotechnology journal · 2023Review
- Molecular insights on CALX-CBD12 interdomain dynamics from MD simulations, RDCs, and SAXS.Biophysical journal · 2021Article
- The diversity of molecular interactions involving intrinsically disordered proteins: A molecular modeling perspective.Computational and structural biotechnology journal · 2021Review
- Probing the dynamic stalk region of the ribosome using solution NMR.Scientific reports · 2019Article
- Localized and Collective Motions in HET-s(218-289) Fibrils from Combined NMR Relaxation and MD Simulation.Angewandte Chemie (International ed. in English) · 2019Article
- How Ricin Damages the Ribosome.Toxins · 2019Review
- Multiplication of Ribosomal P-Stalk Proteins Contributes to the Fidelity of Translation.Molecular and cellular biology · 2017Article
- Combining NMR and small angle X-ray scattering for the study of biomolecular structure and dynamics.Archives of biochemistry and biophysics · 2017Review
- Human ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with a prominent role for P1 C-terminus.Scientific reports · 2017Article
- Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.Chemical reviews · 2016Review
- Do the A subunits contribute to the differences in the toxicity of Shiga toxin 1 and Shiga toxin 2?Toxins · 2015Review
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- Structures of the troponin core domain containing the cardiomyopathy-causing mutants studied by small-angle X-ray scattering.Biophysics and physicobiology · 2015Article
- The dynamic duo: combining NMR and small angle scattering in structural biology.Protein science : a publication of the Protein Society · 2014Review
- HierarchicalJournal of applied crystallography · 2014Article
- NMR methods for structural studies of large monomeric and multimeric proteins.Current opinion in structural biology · 2013Review
- Targeting ricin to the ribosome.Toxicon : official journal of the International Society on Toxinology · 2013Review
- Self-assembly of filamentous amelogenin requires calcium and phosphate: from dimers via nanoribbons to fibrils.Biomacromolecules · 2012Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosomal protein L12 is a two-domain protein that forms dimers mediated by its N-terminal domains. A 20-residue linker separates the N- and C-terminal domains. This linker results in a three-lobe topology with significant flexibility, known to be critical for efficient translation. Here we present an ensemble model of spatial distributions and correlation times for the domain reorientations of L12 that reconciles experimental data from small-angle x-ray scattering and nuclear magnetic resonance. We generated an ensemble of L12 conformations in which the structure of each domain is fixed but the domain orientations are variable. The ensemble reproduces the small-angle x-ray scattering data and the optimized correlation times of its reorientational eigenmodes fit the (15)N relaxation data. The ensemble model reveals intrinsic conformational properties of L12 that help explain its function on the ribosome. The two C-terminal domains sample a large volume and extend further away from the ribosome anchor than expected for a random-chain linker, indicating that the flexible linker has residual order. Furthermore, the distances between each C-terminal domain and the anchor are anticorrelated, indicating that one of them is more retracted on average. We speculate that these properties promote the function of L12 to recruit translation factors and control their activity on the ribosome.
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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.