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| Title | Dynamic Behavior of Trigger Factor on the Ribosome. |
|---|---|
| Journal, issue, pages | J Mol Biol, Vol. 428, Issue 18, Page 3588-3602, Year 2016 |
| Publish date | Sep 11, 2016 |
 Authors | J Deeng / K Y Chan / E O van der Sluis / O Berninghausen / W Han / J Gumbart / K Schulten / B Beatrix / R Beckmann /   |
| PubMed Abstract | Trigger factor (TF) is the only ribosome-associated chaperone in bacteria. It interacts with hydrophobic segments in nascent chain (NCs) as they emerge from the ribosome. TF binds via its N-terminal ...Trigger factor (TF) is the only ribosome-associated chaperone in bacteria. It interacts with hydrophobic segments in nascent chain (NCs) as they emerge from the ribosome. TF binds via its N-terminal ribosome-binding domain (RBD) mainly to ribosomal protein uL23 at the tunnel exit on the large ribosomal subunit. Whereas earlier structural data suggested that TF binds as a rigid molecule to the ribosome, recent comparisons of structural data on substrate-bound, ribosome-bound, and TF in solution from different species suggest that this chaperone is a rather flexible molecule. Here, we present two cryo-electron microscopy structures of TF bound to ribosomes translating an mRNA coding for a known TF substrate from Escherichia coli of a different length. The structures reveal distinct degrees of flexibility for the different TF domains, a conformational rearrangement of the RBD upon ribosome binding, and an increase in rigidity within TF when the NC is extended. Molecular dynamics simulations agree with these data and offer a molecular basis for these observations. |
 External links | J Mol Biol / PubMed:27320387 |
| Methods | EM (single particle) |
| Resolution | 7.7 - 13.1 Å |
| Structure data | EMDB-2695, PDB-4urd:  EMDB-2696:  EMDB-2711: |
| Source |
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 Keywords | ISOMERASE / TRANSLATION / CO-TRANSLATIONAL PROTEIN FOLDING |
escherichia coli (E. coli)