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6HCQ

Structure of the rabbit collided di-ribosome (collided monosome)

This is a non-PDB format compatible entry.
Summary for 6HCQ
Entry DOI10.2210/pdb6hcq/pdb
EMDB information0197
Descriptor28S ribosomal RNA, Ribosomal protein S5, 40S ribosomal protein S6, ... (87 entities in total)
Functional Keywordstranslation, quality control, ribosome
Biological sourceOryctolagus cuniculus
More
Total number of polymer chains85
Total formula weight3462706.10
Authors
Juszkiewicz, S.,Chandrasekaran, V.,Lin, Z.,Kraatz, S.,Ramakrishnan, V.,Hegde, R.S. (deposition date: 2018-08-16, release date: 2018-10-17, Last modification date: 2018-11-14)
Primary citationJuszkiewicz, S.,Chandrasekaran, V.,Lin, Z.,Kraatz, S.,Ramakrishnan, V.,Hegde, R.S.
ZNF598 Is a Quality Control Sensor of Collided Ribosomes.
Mol. Cell, 72:469-481.e7, 2018
Cited by
PubMed Abstract: Aberrantly slow translation elicits quality control pathways initiated by the ubiquitin ligase ZNF598. How ZNF598 discriminates physiologic from pathologic translation complexes and ubiquitinates stalled ribosomes selectively is unclear. Here, we find that the minimal unit engaged by ZNF598 is the collided di-ribosome, a molecular species that arises when a trailing ribosome encounters a slower leading ribosome. The collided di-ribosome structure reveals an extensive 40S-40S interface in which the ubiquitination targets of ZNF598 reside. The paucity of 60S interactions allows for different ribosome rotation states, explaining why ZNF598 recognition is indifferent to how the leading ribosome has stalled. The use of ribosome collisions as a proxy for stalling allows the degree of tolerable slowdown to be tuned by the initiation rate on that mRNA; hence, the threshold for triggering quality control is substrate specific. These findings illustrate how higher-order ribosome architecture can be exploited by cellular factors to monitor translation status.
PubMed: 30293783
DOI: 10.1016/j.molcel.2018.08.037
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6.5 Å)
Structure validation

226707

數據於2024-10-30公開中

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