1QZD

EF-Tu.kirromycin coordinates fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome

Summary for 1QZD

• Entry DOI: 10.2210/pdb1qzd/pdb
• Related: 1OB2 1QZA 1QZB 1QZC 1R2W 1R2X
• EMDB information: 1055
• Descriptor: Elongation factor Tu (1 entity in total)
• Functional Keywords: elongation factor, biosynthetic protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 43239.30

Authors

Valle, M.,Zavialov, A.,Li, W.,Stagg, S.M.,Sengupta, J.,Nielsen, R.C.,Nissen, P.,Harvey, S.C.,Ehrenberg, M.,Frank, J. (deposition date: 2003-09-16, release date: 2003-11-04, Last modification date: 2024-02-14)

Primary citation

Valle, M.,Zavialov, A.,Li, W.,Stagg, S.M.,Sengupta, J.,Nielsen, R.C.,Nissen, P.,Harvey, S.C.,Ehrenberg, M.,Frank, J.
Incorporation of Aminoacyl-tRNA into the Ribosome as seen by Cryo-electron Microscopy
Nat.Struct.Biol., 10:899-906, 2003

PubMed Abstract: Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the ternary complex of aa-tRNA, elongation factor Tu (EF-Tu) and GTP. Here, we present a cryo-electron microscopy (cryo-EM) study, at a resolution of approximately 9 A, showing that during the incorporation of the aa-tRNA into the 70S ribosome of Escherichia coli, the flexibility of aa-tRNA allows the initial codon recognition and its accommodation into the ribosomal A site. In addition, a conformational change observed in the GTPase-associated center (GAC) of the ribosomal 50S subunit may provide the mechanism by which the ribosome promotes a relative movement of the aa-tRNA with respect to EF-Tu. This relative rearrangement seems to facilitate codon recognition by the incoming aa-tRNA, and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu. From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome.

PubMed: 14566331
DOI: 10.1038/nsb1003

Experimental method

ELECTRON MICROSCOPY (10 Å)