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- W2023165276 abstract "Significance The universally conserved signal recognition particle (SRP) and its receptor (FtsY) deliver ∼30% of the proteome to the proper cellular membrane. To ensure proper timing and fidelity of targeting, SRP and FtsY adopt multiple conformations in a GTP-dependent manner. We solved the cryo-EM structure of the SRP–FtsY complex with a GTP analogue in the presence of a ribosome translating a signal sequence (the closed state) at 5.7 Å resolution. We describe the structural basis of ribosome and signal sequence binding by the SRP M domain. We demonstrate that in the closed state the SRP–FtsY GTPase domains are moving away from the ribosomal tunnel exit, allowing for translocon–ribosome interactions to accomplish cotranslational targeting." @default.
- W2023165276 created "2016-06-24" @default.
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- W2023165276 date "2015-03-16" @default.
- W2023165276 modified "2023-10-16" @default.
- W2023165276 title "Ribosome–SRP–FtsY cotranslational targeting complex in the closed state" @default.
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- W2023165276 doi "https://doi.org/10.1073/pnas.1424453112" @default.
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