3ep2 | pdb_00003ep2

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3ep2, resolution 9.00Å (default scene)
Related:	2avy, 2aw4, 1qza, 1ob2, 3eq3, 3eq4
Structural annotation: Resources: InterPro : Ipr020785, Ipr020784, Ipr020783, Ipr006519, Ipr000911, Ipr012340, Ipr016027, Ipr006032, Ipr005679, Ipr004161, Ipr004160, Ipr000795, Ipr004541, Ipr005225, Ipr009001, Ipr009000 Pfam : PF03946, PF00298, PF00164
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
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

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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

• Ribosomal protein L11
• Ribosomal protein S12

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