Structural highlights
Function
[RL23_ECO57] One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
Publication Abstract from PubMed
The E.coli ribosome exit tunnel can accommodate small folded proteins, while larger ones fold outside. It remains unclear, however, to what extent the geometry of the tunnel influences protein folding. Here, using E. coli ribosomes with deletions in loops in proteins uL23 and uL24 that protrude into the tunnel, we investigate how tunnel geometry determines where proteins of different sizes fold. We find that a 29-residue zinc-finger domain normally folding close to the uL23 loop folds deeper in the tunnel in uL23 Dloop ribosomes, while two ~100-residue protein normally folding close to the uL24 loop near the tunnel exit port fold at deeper locations in uL24 Dloop ribosomes, in good agreement with results obtained by coarse-grained molecular dynamics simulations. This supports the idea that cotranslational folding commences once a protein domain reaches a location in the exit tunnel where there is sufficient space to house the folded structure.
The shape of the ribosome exit tunnel affects cotranslational protein folding.,Kudva R, Tian P, Pardo-Avila F, Carroni M, Best R, Bernstein HD, von Heijne G Elife. 2018 Nov 26;7. pii: 36326. doi: 10.7554/eLife.36326. PMID:30475203[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kudva R, Tian P, Pardo-Avila F, Carroni M, Best R, Bernstein HD, von Heijne G. The shape of the ribosome exit tunnel affects cotranslational protein folding. Elife. 2018 Nov 26;7. pii: 36326. doi: 10.7554/eLife.36326. PMID:30475203 doi:http://dx.doi.org/10.7554/eLife.36326
