Structural highlights
Function
RS15_THET8 One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA (By similarity).[HAMAP-Rule:MF_01343] Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.[HAMAP-Rule:MF_01343]
Publication Abstract from PubMed
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(5) 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.
Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination.,Zeng F, Jin H Sci Rep. 2018 Feb 5;8(1):2349. doi: 10.1038/s41598-018-20107-8. PMID:29403017[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zeng F, Jin H. Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination. Sci Rep. 2018 Feb 5;8(1):2349. doi: 10.1038/s41598-018-20107-8. PMID:29403017 doi:http://dx.doi.org/10.1038/s41598-018-20107-8
