Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 106, Issue 4, Pages 1063-1068Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0811370106
Keywords
decoding; GTPase; flexible fitting; cryo-EM; ternary complex
Categories
Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NCRR NIH HHS [P41 RR001219, P41 RR005969, P41-RR01219, P41-RR05969] Funding Source: Medline
- NIGMS NIH HHS [R01 GM070768, R37-GM29169, R01 GM055440, R01-GM55440, R37 GM029169, R01-GM070768] Funding Source: Medline
- Direct For Mathematical & Physical Scien
- Division Of Physics [0822613] Funding Source: National Science Foundation
Ask authors/readers for more resources
In translation, elongation factor Tu (EF-Tu) molecules deliver aminoacyl-tRNAs to the mRNA-programmed ribosome. The GTPase activity of EF-Tu is triggered by ribosome-induced conformational changes of the factor that play a pivotal role in the selection of the cognate aminoacyl-tRNAs. We present a 6.7-angstrom cryo-electron microscopy map of the aminoacyl-tRNA (.) EF-Tu (.) GDP (.) kirromycin-bound Escherichia coli ribosome, together with an atomic model of the complex obtained through molecular dynamics flexible fitting. The model reveals the conformational changes in the conserved GTPase switch regions of EF-Tu that trigger hydrolysis of GTP, along with key interactions, including those between the sarcin-ricin loop and the P loop of EF-Tu, and between the effector loop of EF-Tu and a conserved region of the 16S rRNA. Our data suggest that GTP hydrolysis on EF-Tu is controlled through a hydrophobic gate mechanism.
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