Journal
EMBO JOURNAL
Volume 21, Issue 13, Pages 3557-3567Publisher
WILEY
DOI: 10.1093/emboj/cdf326
Keywords
decoding; electron microscopy; elongation factor Tu; ribosome; tRNA
Categories
Funding
- NCRR NIH HHS [P41 RR001219, P41 RR01219] Funding Source: Medline
- NIGMS NIH HHS [R01 GM055440, R01 GM61576, R37 GM029169, R01 GM55440, R37 GM29169, R01 GM061576] Funding Source: Medline
Ask authors/readers for more resources
During the elongation cycle of protein biosynthesis, the specific amino acid coded for by the mRNA is delivered by a complex that is comprised of the cognate aminoacyl-tRNA, elongation factor Tu and GTP. As this ternary complex binds to the ribosome, the anticodon end of the tRNA reaches the decoding center in the 30S subunit. Here we present the cryo- electron microscopy (EM) study of an Escherichia coli 70S ribosome-bound ternary complex stalled with an antibiotic, kirromycin. In the cryo-EM map the anticodon arm of the tRNA presents a new conformation that appears to facilitate the initial codon-anticodon interaction. Furthermore, the elbow region of the tRNA is seen to contact the GTPase-associated center on the 50S subunit of the ribosome, suggesting an active role of the tRNA in the transmission of the signal prompting the GTP hydrolysis upon codon recognition.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available