5A8L

Human eRF1 and the hCMV nascent peptide in the translation termination complex

Summary for 5A8L

• Entry DOI: 10.2210/pdb5a8l/pdb
• EMDB information: 3099
• Descriptor: 28S RIBOSOMAL RNA, HUMAN 18S RIBOSOMAL RNA, 60S RIBOSOMAL PROTEIN L17, ... (9 entities in total)
• Functional Keywords: human, 80s, ribosome, erf1, translation
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm: P62495
• Total number of polymer chains: 9
• Total formula weight: 2375320.31

Authors

Matheisl, S.,Berninghausen, O.,Becker, T.,Beckmann, R. (deposition date: 2015-07-16, release date: 2015-12-02, Last modification date: 2024-05-08)

Primary citation

Matheisl, S.,Berninghausen, O.,Becker, T.,Beckmann, R.
Structure of a Human Translation Termination Complex.
Nucleic Acids Res., 43:8615-, 2015

PubMed Abstract: In contrast to bacteria that have two release factors, RF1 and RF2, eukaryotes only possess one unrelated release factor eRF1, which recognizes all three stop codons of the mRNA and hydrolyses the peptidyl-tRNA bond. While the molecular basis for bacterial termination has been elucidated, high-resolution structures of eukaryotic termination complexes have been lacking. Here we present a 3.8 Å structure of a human translation termination complex with eRF1 decoding a UAA(A) stop codon. The complex was formed using the human cytomegalovirus (hCMV) stalling peptide, which perturbs the peptidyltransferase center (PTC) to silence the hydrolysis activity of eRF1. Moreover, unlike sense codons or bacterial stop codons, the UAA stop codon adopts a U-turn-like conformation within a pocket formed by eRF1 and the ribosome. Inducing the U-turn conformation for stop codon recognition rationalizes how decoding by eRF1 includes monitoring geometry in order to discriminate against sense codons.

PubMed: 26384426
DOI: 10.1093/NAR/GKV909

Experimental method

ELECTRON MICROSCOPY (3.8 Å)