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

Summary for 1LS2

• Entry DOI: 10.2210/pdb1ls2/pdb
• Related: 1EFC 1EXM 1lu3 1TTT
• EMDB information: 1045
• Descriptor: Phenylalanine transfer RNA, Elongation Factor Tu (2 entities in total)
• Functional Keywords: ef-tu, ternary complex, cryo-em, 70s e.coli ribosome, translation-rna complex, translation/rna
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 67757.87

Authors

Valle, M.,Sengupta, J.,Swami, N.K.,Grassucci, R.A.,Burkhardt, N.,Nierhaus, K.H.,Agrawal, R.K.,Frank, J. (deposition date: 2002-05-16, release date: 2002-06-26, Last modification date: 2024-02-14)

Primary citation

Valle, M.,Sengupta, J.,Swami, N.K.,Grassucci, R.A.,Burkhardt, N.,Nierhaus, K.H.,Agrawal, R.K.,Frank, J.
Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process.
EMBO J., 21:3557-3567, 2002

PubMed Abstract: 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.

PubMed: 12093756
DOI: 10.1093/emboj/cdf326

Experimental method

ELECTRON MICROSCOPY (16.8 Å)