The SRP-SR co-translational targeting complex in the closed state displays flexible NG-domains and a defined M-domain with signal sequence
نویسندگان
چکیده
Affiliations: European Molecular Biology Laboratory, Grenoble Outstation, Grenoble, 38042 France Unit for Virus Host-Cell Interactions, Univ. Grenoble Alpes-EMBL-CNRS, Grenoble, 38042 France Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125 School of Biochemistry, University of Bristol, Bristol, BS8 1TD, United Kingdom Current address: Institute of Structural and Molecular Biology, Birkbeck College, London, WC1E 7HX, United Kingdom
منابع مشابه
Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome
During co-translational protein targeting, the signal recognition particle (SRP) binds to the translating ribosome displaying the signal sequence to deliver it to the SRP receptor (SR) on the membrane, where the signal peptide is transferred to the translocon. Using electron cryo-microscopy, we have determined the structure of a quaternary complex of the translating Escherichia coli ribosome, t...
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