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PDBsum entry 4crm
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References listed in PDB file
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Key reference
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Title
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Cryoelectron microscopic structures of eukaryotic translation termination complexes containing erf1-Erf3 or erf1-Abce1.
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Authors
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A.Preis,
A.Heuer,
C.Barrio-Garcia,
A.Hauser,
D.E.Eyler,
O.Berninghausen,
R.Green,
T.Becker,
R.Beckmann.
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Ref.
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Cell Rep, 2014,
8,
59-65.
[DOI no: ]
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PubMed id
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Abstract
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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.
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