Abstract:
: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-A cryo-electron microscopy map of the aminoacyl-tRNA x EF-Tu x GDP x 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.
journal_name
Proc Natl Acad Sci U S Aauthors
Villa E,Sengupta J,Trabuco LG,LeBarron J,Baxter WT,Shaikh TR,Grassucci RA,Nissen P,Ehrenberg M,Schulten K,Frank Jdoi
10.1073/pnas.0811370106subject
Has Abstractpub_date
2009-01-27 00:00:00pages
1063-8issue
4eissn
0027-8424issn
1091-6490pii
0811370106journal_volume
106pub_type
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