{"doi":"10.1038/ncomms10471","title":"Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon","abstract":"<jats:title>Abstract</jats:title>\n                  <jats:p>\n                    Co-translational protein targeting to membranes is a universally conserved process. Central steps include cargo recognition by the signal recognition particle and handover to the Sec translocon. Here we present snapshots of key co-translational-targeting complexes solved by cryo-electron microscopy at near-atomic resolution, establishing the molecular contacts between the\n                    <jats:italic>Escherichia coli</jats:italic>\n                    translating ribosome, the signal recognition particle and the translocon. Our results reveal the conformational changes that regulate the latching of the signal sequence, the release of the heterodimeric domains of the signal recognition particle and its receptor, and the handover of the signal sequence to the translocon. We also observe that the signal recognition particle and the translocon insert-specific structural elements into the ribosomal tunnel to remodel it, possibly to sense nascent chains. Our work provides structural evidence for a conformational state of the signal recognition particle and its receptor primed for translocon binding to the ribosome–nascent chain complex.\n                  </jats:p>","journal":"Nature Communications","year":2016,"id":37950,"datarank":3.500406951865817,"base_score":4.700480365792417,"endowment":4.700480365792417,"self_citation_contribution":0.7050720548688626,"citation_network_contribution":2.7953348969969545,"self_endowment_contribution":0.7050720548688626,"citer_contribution":2.7953348969969545,"corpus_percentile":null,"corpus_rank":null,"citation_count":109,"citer_count":103,"citers_with_citation_signal":91,"citers_with_endowment":91,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":189114,"name":"Daniel Boehringer","orcid":null,"position":1,"is_corresponding":false},{"id":189115,"name":"Marc Leibundgut","orcid":null,"position":2,"is_corresponding":false},{"id":189116,"name":"Nenad Ban","orcid":null,"position":3,"is_corresponding":false},{"id":17834,"name":"Ahmad Jomaa","orcid":"0000-0002-5543-7942","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":4.700480365792417,"endowment":4.700480365792417,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"26804923","pmcid":"PMC4737761","openalex_id":"https://openalex.org/W2264866006","authors":[],"funders":[{"funder_name":"Swiss National Science Foundation","grant_id":"250071","title":"Structural studies of the eukaryotic ribosome by X-ray crystallography"}],"total_grants":1,"fwci":9.749,"citation_percentile":0.98453014,"influential_citations":9,"citation_trend":[{"year":2016,"count":11},{"year":2017,"count":10},{"year":2018,"count":16},{"year":2019,"count":16},{"year":2020,"count":6},{"year":2021,"count":12},{"year":2022,"count":13},{"year":2023,"count":6},{"year":2024,"count":8},{"year":2025,"count":8},{"year":2026,"count":3}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://www.nature.com/articles/ncomms10471.pdf","host_type":"journal"},{"url":"https://www.nature.com/articles/ncomms10471.pdf","host_type":"GOLD"},{"url":"https://www.nature.com/articles/ncomms10471.pdf","host_type":"publisher"},{"url":"https://www.nature.com/articles/ncomms10471","host_type":"publisher"},{"url":"https://doi.org/10.1038/ncomms10471","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/26804923","host_type":"repository"},{"url":"https://doaj.org/article/d624a79fa14545299654ce329de54142","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/4737761","host_type":"repository"},{"url":"http://hdl.handle.net/20.500.11850/112526","host_type":"repository"},{"url":"https://doi.org/10.3929/ethz-b-000112526","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC4737761","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC4737761?pdf=render","host_type":"Europe_PMC"},{"url":"https://dx.doi.org/10.3929/ethz-b-000112526","host_type":""},{"url":"http://dx.doi.org/10.1038/ncomms10471","host_type":""},{"url":"https://dx.doi.org/10.1038/ncomms10471","host_type":""},{"url":"https://sonar.ch/global/documents/143421","host_type":""}],"fields_of_study":["RNA and protein synthesis mechanisms","Advanced Electron Microscopy Techniques and Applications","Force Microscopy Techniques and Applications","Medicine","Biology","0301 basic medicine","0303 health sciences","03 medical and health sciences","Codon","Cryoelectron Microscopy","Escherichia coli","Escherichia coli Proteins","Models, Molecular","Protein Binding","Protein Biosynthesis","Protein Transport","RNA, Messenger","Receptors, Cytoplasmic and Nuclear","Receptors, Peptide","Ribosomes","Signal Recognition Particle","Transcription Factors"],"mesh_terms":["Codon","Escherichia coli","Models, Molecular","Protein Binding","Ribosomes","RNA, Messenger","Transcription Factors","Protein Biosynthesis","Receptors, Peptide","Receptors, Cytoplasmic and Nuclear","Signal Recognition Particle","Cryoelectron Microscopy","Protein Transport","Escherichia coli Proteins"],"keywords":["Translocon","Signal recognition particle","Signal recognition particle receptor","Signal peptide","Ribosome","Translation (biology)","Sequence (biology)","Biology","Cell biology","Biophysics","Biochemistry","Membrane protein","Peptide sequence","RNA","Membrane","Models, Molecular","Receptors, Peptide","Science","Escherichia coli Proteins","Q","Cryoelectron Microscopy","Receptors, Cytoplasmic and Nuclear","Article","Protein Transport","Protein Biosynthesis","Escherichia coli","RNA, Messenger","Codon","Ribosomes","Protein Binding","Transcription Factors"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. 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