PDBsum entry 4crm

Translation

PDB id: 4crm

Contents

Protein chains

608 a.a.

282 a.a.

Ligands

ATP

SF4 ×2

ADP

Metals

_MG

Waters ×1

PDB id:

4crm

Name:

Translation

Title:

Cryo-em of a pre-recycling complex with erf1 and abce1

Structure:

Translation initiation factor rli1. Chain: p. Synonym: atp-binding cassette sub-family e member rli1, rnase l inhibitor, abce1 in ribosome bound erf1-abce1-adpnp complex. Engineered: yes. Eukaryotic peptide chain release factor subunit 1. Chain: x. Synonym: eukaryotic release factor 1, erf1, omnipotent suppressor protein 1, erf1 in ribosome-bound erf1-abce1-adpnp complex.

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562

Authors:

A.Preis,A.Heuer,C.Barrio-Garcia,A.Hauser,D.Eyler,O.Berninghausen, R.Green,T.Becker,R.Beckmann

Key ref:

A.Preis et al. (2014). Cryoelectron microscopic structures of eukaryotic translation termination complexes containing eRF1-eRF3 or eRF1-ABCE1. Cell Rep, 8, 59-65. PubMed id: 25001285 DOI: 10.1016/j.celrep.2014.04.058

Date:

28-Feb-14 Release date: 23-Jul-14

Protein chain

Q03195  (RLI1_YEAST) -  Translation initiation factor RLI1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 608 a.a.

Struc: 608 a.a.

Protein chain

P12385  (ERF1_YEAST) -  Eukaryotic peptide chain release factor subunit 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 437 a.a.

Struc: 282 a.a.

Enzyme reactions

• Enzyme class: Chains P, X: E.C.?

DOI no: 10.1016/j.celrep.2014.04.058

Cell Rep 8:59-65 (2014)

PubMed id: 25001285

Cryoelectron microscopic structures of eukaryotic translation termination complexes containing eRF1-eRF3 or eRF1-ABCE1.

A.Preis, A.Heuer, C.Barrio-Garcia, A.Hauser, D.E.Eyler, O.Berninghausen, R.Green, T.Becker, R.Beckmann.

ABSTRACT

Termination and ribosome recycling are essential processes in translation. In eukaryotes, a stop codon in the ribosomal A site is decoded by a ternary complex consisting of release factors eRF1 and guanosine triphosphate (GTP)-bound eRF3. After GTP hydrolysis, eRF3 dissociates, and ABCE1 can bind to eRF1-loaded ribosomes to stimulate peptide release and ribosomal subunit dissociation. Here, we present cryoelectron microscopic (cryo-EM) structures of a pretermination complex containing eRF1-eRF3 and a termination/prerecycling complex containing eRF1-ABCE1. eRF1 undergoes drastic conformational changes: its central domain harboring the catalytically important GGQ loop is either packed against eRF3 or swung toward the peptidyl transferase center when bound to ABCE1. Additionally, in complex with eRF3, the N-terminal domain of eRF1 positions the conserved NIKS motif proximal to the stop codon, supporting its suggested role in decoding, yet it appears to be delocalized in the presence of ABCE1. These results suggest that stop codon decoding and peptide release can be uncoupled during termination.