Structure (London), 2005-11, Vol.13 (11), p.1685-1694
2005
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- Autor(en) / Beteiligte
- Titel
- The Binding Mode of the Trigger Factor on the Ribosome: Implications for Protein Folding and SRP Interaction
- Ist Teil von
- Structure (London), 2005-11, Vol.13 (11), p.1685-1694
- Ort / Verlag
- United States: Elsevier Inc
- Erscheinungsjahr
- 2005
- Quelle
- Free E-Journal (出版社公開部分のみ）
- Beschreibungen/Notizen
- This study presents the X-ray structure of the N-terminal binding domain of the D. radiodurans trigger factor (TF) in complex with the D. radiodurans large ribosomal subunit. At 3.35 Å, a complete description of the interactions with ribosomal proteins L23, L29, and 23S rRNA are disclosed, many of which differ from those found previously for a heterologous bacterial-archaeal TF-ribosome complex. The β hairpin loop of eubacterial L24, which is shorter in archaeal ribosomes, contacts the TF and severely diminishes the molecular cradle proposed to exist between the TF and ribosome. Bound to the ribosome, TF exposes a hydrophobic crevice large enough to accommodate the nascent polypeptide chain. Superimposition of the full-length TF and the signal-recognition particle (SRP) onto the complex shows that simultaneous cohabitation is possible, in agreement with biochemical data, and suggests a model for the interplay of TF, SRP, and the nascent chain during translation.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0969-2126eISSN: 1878-4186DOI: 10.1016/j.str.2005.08.007Titel-ID: cdi_proquest_miscellaneous_68770466
- Format
- –
- Schlagworte
- Amino Acid Sequence, Bacterial Proteins - chemistry, Bacterial Proteins - metabolism, Bacterial Proteins - physiology, Binding Sites, Deinococcus - chemistry, Deinococcus - genetics, Deinococcus - physiology, Hydrophobic and Hydrophilic Interactions, Molecular Chaperones - chemistry, Molecular Chaperones - metabolism, Molecular Chaperones - physiology, Molecular Sequence Data, Peptides - chemistry, Peptides - metabolism, Peptides - physiology, Protein Binding, Protein Folding, Protein Structure, Tertiary, Ribosomal Proteins - chemistry, Ribosomal Proteins - metabolism, Ribosomal Proteins - physiology, Signal Recognition Particle - chemistry, Signal Recognition Particle - metabolism, Signal Recognition Particle - physiology