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5LL6

Structure of the 40S ABCE1 post-splitting complex in ribosome recycling and translation initiation

Summary for 5LL6
Entry DOI10.2210/pdb5ll6/pdb
EMDB information4071
Descriptor18S ribosomal RNA, 40S ribosomal protein S11-A, 40S ribosomal protein S13, ... (23 entities in total)
Functional Keywordsabce1, ribosome, recycling, 40s
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Total number of polymer chains20
Total formula weight991672.15
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 citationHeuer, 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: 28368393
DOI: 10.1038/nsmb.3396
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

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数据于2025-07-23公开中

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