Nat Struct Biol. 2003 Nov;10(11):899-906. Epub 2003 Oct 19.

Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy.

Valle M, Zavialov A, Li W, Stagg SM, Sengupta J, Nielsen RC, Nissen P, Harvey SC, Ehrenberg M, Frank J.

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Howard Hughes Medical Institute, Health Research, Inc. at the Wadsworth Center, Empire State Plaza, Albany, New York 12201-0509, USA.

Erratum in

Nat Struct Biol. 2003 Dec;10(12):1074.

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.

PMID:: 14566331; [PubMed - indexed for MEDLINE]

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Cited by 65 PubMed Central articles

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Structures reported by this article

Coordinates Of L11 With 58nts Of 23s Rrna Fitted Into The Cryo-Em Map Of Ef-Tu Ternary Complex (Gdp.Kirromycin) Bound 70s Ribosomeÿ

PDB: 1R2X

Source: Thermotoga maritima, synthetic construct

Method: Cryo-Electron Microscopy

Resolution: 9 Å

See all 6 structures...

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