ArticleThe EMBO journal1994
Crystal structure of the ribosomal protein S6 from Thermus thermophilus.
Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 147 citations in OpenAlex.
- Design and characterization of a protein fold switching network.Nature communications · 2023Article
- Reversible switching between two common protein folds in a designed system using only temperature.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Quantitating denaturation by formic acid: imperfect repeats are essential to the stability of the functional amyloid protein FapC.The Journal of biological chemistry · 2020Article
- Network Connectivity, Centrality and Fragmentation in the Greek-Key Protein Topology.The protein journal · 2019Article
- Genetic correlation network prediction of forest soil microbial functional organization.The ISME journal · 2018Article
- Constructing sequence-dependent protein models using coevolutionary information.Protein science : a publication of the Protein Society · 2016Article
- The response of Greek key proteins to changes in connectivity depends on the nature of their secondary structure.Journal of molecular biology · 2015Article
- Sequence analysis on the information of folding initiation segments in ferredoxin-like fold proteins.BMC structural biology · 2014Article
- Structural similarity between defense peptide from wheat and scorpion neurotoxin permits rational functional design.The Journal of biological chemistry · 2014Article
- Probing the protein-folding mechanism using denaturant and temperature effects on rate constants.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Elongation factor G bound to the ribosome in an intermediate state of translocation.Science (New York, N.Y.) · 2013Article
- Folding without charges.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Trimming down a protein structure to its bare foldons: spatial organization of the cooperative unit.The Journal of biological chemistry · 2012Article
- Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Solution structures and backbone dynamics of the ribosomal protein S6 and its permutant P(54-55).Protein science : a publication of the Protein Society · 2010Article
- The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms.Nature structural & molecular biology · 2009Review
- Identification of the minimal protein-folding nucleus through loop-entropy perturbations.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The amino acid sequence and crystal structure of the ribosomal protein S6 from the small ribosomal subunit of Thermus thermophilus have been determined. S6 is a small protein with 101 amino acid residues. The 3D structure, which was determined to 2.0 A resolution, consists of a four-stranded anti-parallel beta-sheet with two alpha-helices packed on one side. Similar folding patterns have been observed for other ribosomal proteins and may suggest an original RNA-interacting motif. Related topologies are also found in several other nucleic acid-interacting proteins and based on the assumption that the structure of the ribosome was established early in the molecular evolution, the possibility that an ancestral RNA-interacting motif in ribosomal proteins is the evolutionary origin for the nucleic acid-interacting domain in large classes of ribonucleic acid binding proteins should be considered.
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