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• W2095062022 endingPage "1556" @default.
• W2095062022 startingPage "1547" @default.
• W2095062022 abstract "The exit tunnel region of the ribosome is well established as a focal point for interaction between the components that guide the fate of nascent polypeptides. One of these, the chaperone trigger factor (TF), associates with the 50S ribosomal subunit through its N-terminal domain. Targeting of TF to ribosomes is crucial to achieve its remarkable efficiency in protein folding. A similar tight coupling to translation is found in signal recognition particle (SRP)-dependent protein translocation. Here, we report crystal structures of the E. coli TF ribosome binding domain. TF is structurally related to the Hsp33 chaperone but has a prominent ribosome anchor located as a tip of the molecule. This tip includes the previously established unique TF signature motif. Comparison reveals that this feature is not found in SRP structures. We identify a conserved helical kink as a hallmark of the TF structure that is most likely critical to ensure ribosome association." @default.
• W2095062022 created "2016-06-24" @default.
• W2095062022 creator A5000797815 @default.
• W2095062022 creator A5091273265 @default.
• W2095062022 date "2003-12-01" @default.
• W2095062022 modified "2023-09-23" @default.
• W2095062022 title "Chaperone Binding at the Ribosomal Exit Tunnel" @default.
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• W2095062022 doi "https://doi.org/10.1016/j.str.2003.11.003" @default.
• W2095062022 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14656439" @default.
• W2095062022 hasPublicationYear "2003" @default.
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