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| Title | Structure of the 40S-ABCE1 post-splitting complex in ribosome recycling and translation initiation. |
|---|---|
| Journal, issue, pages | Nat Struct Mol Biol, Vol. 24, Issue 5, Page 453-460, Year 2017 |
| Publish date | Apr 3, 2017 |
 Authors | André Heuer / Milan Gerovac / Christian Schmidt / Simon Trowitzsch / Anne Preis / Peter Kötter / Otto Berninghausen / Thomas Becker / Roland Beckmann / Robert Tampé /  |
| PubMed Abstract | The essential ATP-binding cassette protein ABCE1 splits 80S ribosomes into 60S and 40S subunits after canonical termination or quality-control-based mRNA surveillance processes. However, the ...The essential ATP-binding cassette protein ABCE1 splits 80S ribosomes into 60S and 40S subunits after canonical termination or quality-control-based mRNA surveillance processes. However, the underlying splitting mechanism remains enigmatic. Here, we present a cryo-EM structure of the yeast 40S-ABCE1 post-splitting complex at 3.9-Å resolution. Compared to the pre-splitting state, we observe repositioning of ABCE1's iron-sulfur cluster domain, which rotates 150° into a binding pocket on the 40S subunit. This repositioning explains a newly observed anti-association activity of ABCE1. Notably, the movement implies a collision with A-site factors, thus explaining the splitting mechanism. Disruption of key interactions in the post-splitting complex impairs cellular homeostasis. Additionally, the structure of a native post-splitting complex reveals ABCE1 to be part of the 43S initiation complex, suggesting a coordination of termination, recycling, and initiation. |
 External links | Nat Struct Mol Biol / PubMed:28368393 |
| Methods | EM (single particle) |
| Resolution | 3.9 - 14.0 Å |
| Structure data |  EMDB-3452: |
| Chemicals |  ChemComp-SF4:  ChemComp-ANP:  ChemComp-MG: |
| Source |
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 Keywords |  RIBOSOME / ABCE1 / recycling / 40S |
