5LL6
Structure of the 40S ABCE1 post-splitting complex in ribosome recycling and translation initiation
Summary for 5LL6
Entry DOI | 10.2210/pdb5ll6/pdb |
EMDB information | 4071 |
Descriptor | 18S ribosomal RNA, 40S ribosomal protein S11-A, 40S ribosomal protein S13, ... (23 entities in total) |
Functional Keywords | abce1, ribosome, recycling, 40s |
Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
Total number of polymer chains | 20 |
Total formula weight | 991672.15 |
Authors | Heuer, A.,Gerovac, M.,Schmidt, C.,Trowitzsch, S.,Preis, A.,Koetter, P.,Berninghausen, O.,Becker, T.,Beckmann, R.,Tampe, R. (deposition date: 2016-07-26, release date: 2017-04-12, Last modification date: 2024-05-08) |
Primary citation | Heuer, A.,Gerovac, M.,Schmidt, C.,Trowitzsch, S.,Preis, A.,Kotter, P.,Berninghausen, O.,Becker, T.,Beckmann, R.,Tampe, R. Structure of the 40S-ABCE1 post-splitting complex in ribosome recycling and translation initiation. Nat. Struct. Mol. Biol., 24:453-460, 2017 Cited by 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 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. PubMed: 28368393DOI: 10.1038/nsmb.3396 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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