9Q7Q

ABCE1-eRF1-RNC-AMD1C

This is a non-PDB format compatible entry.

Summary for 9Q7Q

• Entry DOI: 10.2210/pdb9q7q/pdb
• EMDB information: 72314
• Descriptor: Ribosomal protein S27a, Ribosomal protein L8, Ribosomal protein L3, ... (88 entities in total)
• Functional Keywords: amd1, ribosome stalling, arresting peptide, erf1, abce1, ribosome
• Biological source: Oryctolagus cuniculus (rabbit); More
• Total number of polymer chains: 86
• Total formula weight: 5559006.04

Authors

Maldosevic, E.,Jomaa, A. (deposition date: 2025-08-25, release date: 2026-03-04, Last modification date: 2026-04-08)

Primary citation

Maldosevic, E.,Boiocchi, F.S.,Swirski, M.I.,Meiklejohn, K.A.,Yordanova, M.M.,Baranov, P.V.,Jomaa, A.
Mechanism of ribosome stalling by the AMD1 C-terminal tail arrest peptide.
Sci Adv, 12:eaec5067-eaec5067, 2026

PubMed Abstract: encodes adenosylmethionine decarboxylase 1 (AMD1), a key enzyme in polyamine biosynthesis. A subset of ribosomes translating the coding sequence read through the stop codon and pause at a second in-frame stop 384 nucleotides downstream, producing a conserved C-terminal extension (C-tail). Despite growing evidence that such cis-acting elements regulate translation of their genes, the molecular mechanism by which the C-tail mediates ribosome stalling remains unclear. Here, we determined the structure of the ribosome nascent chain complex paused by the AMD1 C-tail which traps eukaryotic release factor 1 (eRF1) with the ATP-binding cassette subfamily E member 1 (ABCE1). The nascent chain forms a molecular clamp that positions an arginine hook in the peptidyl-transferase center, occluding the accommodation of the eRF1 GGQ motif thereby hampering translation termination. Analysis of aggregated ribosome profiling data revealed several genes with a pattern of stop codon readthrough followed by ribosome stalling at a specific location, suggesting that regulatory readthrough-stall mechanisms may not be limited to .

PubMed: 41894501
DOI: 10.1126/sciadv.aec5067

Experimental method

ELECTRON MICROSCOPY (2.86 Å)