Jomaa A Boehringer D Leibundgut M Ban N 2016 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 Escherichia coli 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. application/pdf https://sonar.ch/global/documents/143421 eng info:eu-repo/semantics/altIdentifier/doi/10.1038/ncomms10471 info:eu-repo/semantics/altIdentifier/pmid/26804923 info:eu-repo/semantics/openAccess Nature communications. - 2016 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 Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon. http://purl.org/coar/resource_type/c_6501