1LS2: Fitting Of Ef-Tu And Trna In The Low Resolution Cryo-Em Map Of An Ef-Tu Ternary Complex (Gdp And Kirromycin) Bound To E. Coli 70s Ribosome

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.
PDB ID: 1LS2Download
MMDB ID: 19983
PDB Deposition Date: 2002/5/16
Updated in MMDB: 2012/10
Experimental Method:
electron microscopy
Resolution: 16.8  Å
Source Organism:
Saccharomyces cerevisiae
Similar Structures:
Biological Unit for 1LS2: dimeric; determined by author
Molecular Components in 1LS2
Label Count Molecule
Protein (1 molecule)
Elongation Factor TU
Molecule annotation
Nucleotide(1 molecule)
Phenylalanine Transfer RNA
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB