3ep2: Difference between revisions

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[[Image:3ep2.png|left|200px]]
[[Image:3ep2.png|left|200px]]


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===Model of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM===
===Model of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM===


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Revision as of 01:13, 27 July 2012


Drag the structure with the mouse to rotate
3ep2, resolution 9.00Å (default scene)
Related: 2avy, 2aw4, 1qza, 1ob2, 3eq3, 3eq4
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Model of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM

Publication Abstract from PubMed

The accuracy of ribosomal translation is achieved by an initial selection and a proofreading step, mediated by EF-Tu, which forms a ternary complex with aminoacyl(aa)-tRNA. To study the binding modes of different aa-tRNAs, we compared cryo-EM maps of the kirromycin-stalled ribosome bound with ternary complexes containing Phe-tRNA(Phe), Trp-tRNA(Trp), or Leu-tRNA(LeuI). The three maps suggest a common binding manner of cognate aa-tRNAs in their specific binding with both the ribosome and EF-Tu. All three aa-tRNAs have the same 'loaded spring' conformation with a kink and twist between the D-stem and anticodon stem. The three complexes are similarly integrated in an interaction network, extending from the anticodon loop through h44 and protein S12 to the EF-Tu-binding CCA end of aa-tRNA, proposed to signal cognate codon-anticodon interaction to the GTPase centre and tune the accuracy of aa-tRNA selection.

Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM., Li W, Agirrezabala X, Lei J, Bouakaz L, Brunelle JL, Ortiz-Meoz RF, Green R, Sanyal S, Ehrenberg M, Frank J, EMBO J. 2008 Dec 17;27(24):3322-31. Epub 2008 Nov 20. PMID:19020518

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3ep2 is a 9 chain structure of Ribosomal protein L11 and Ribosomal protein S12 with sequence from Escherichia coli k12. Full crystallographic information is available from OCA.

See Also

Reference

  1. Li W, Agirrezabala X, Lei J, Bouakaz L, Brunelle JL, Ortiz-Meoz RF, Green R, Sanyal S, Ehrenberg M, Frank J. Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM. EMBO J. 2008 Dec 17;27(24):3322-31. Epub 2008 Nov 20. PMID:19020518 doi:10.1038/emboj.2008.243

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