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TitleConformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination.
Journal, issue, pagesSci Rep, Vol. 8, Issue 1, Page 2349, Year 2018
Publish dateFeb 5, 2018
AuthorsFuxing Zeng / Hong Jin /
PubMed AbstractThe universally conserved Gly-Gly-Gln (GGQ) tripeptide in release factors or release factor-like surveillance proteins is required to catalyze the release of nascent peptide in the ribosome. The ...The universally conserved Gly-Gly-Gln (GGQ) tripeptide in release factors or release factor-like surveillance proteins is required to catalyze the release of nascent peptide in the ribosome. The glutamine of the GGQ is methylated post-translationally at the N position in vivo; this covalent modification is essential for optimal cell growth and efficient translation termination. However, the precise conformation of the methylated-GGQ tripeptide in the ribosome remains unknown. Using cryoEM and X-ray crystallography, we report the conformation of methylated-GGQ in the peptidyl transferase center of the ribosome during canonical translational termination and co-translation quality control. It has been suggested that the GGQ motif arose independently through convergent evolution among otherwise unrelated proteins that catalyze peptide release. The requirement for this tripeptide in the highly conserved peptidyl transferase center suggests that the conformation reported here is likely shared during termination of protein synthesis in all domains of life.
External linksSci Rep / PubMed:29403017 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.1 - 3.24 Å
Structure data

7340

6c4h

EMDB-7340, PDB-6c4h:
Conformation of methylated GGQ in the peptidyl transferase center during translation termination (PTC region)
Method: EM (single particle) / Resolution: 3.1 Å

7341

6c4i

EMDB-7341, PDB-6c4i:
Conformation of methylated GGQ in the peptidyl transferase center during translation termination
Method: EM (single particle) / Resolution: 3.24 Å

PDB-6c5l:
Conformation of methylated GGQ in the Peptidyl Transferase Center during translation termination (T. thermophilus)
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • escherichia coli (E. coli)
  • thermus thermophilus (bacteria)
KeywordsRIBOSOMAL PROTEIN/RNA / nonstop / termination / ArfA / RF2 / methylation / RIBOSOMAL PROTEIN-RNA complex / RIBOSOME / methylated RF2 / translation termination

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