3ep2

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3ep2, resolution 9.00Å () | |||||||||
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Related: | 2avy, 2aw4, 1qza, 1ob2, 3eq3, 3eq4 | ||||||||
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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-EMModel of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM
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 StructureAbout this Structure
3EP2 is a Protein complex structure of sequences from Escherichia coli k12. Full crystallographic information is available from OCA.
ReferenceReference
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 Nov 20. PMID:19020518 [[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
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OCA- Escherichia coli k12
- Protein complex
- A/t-trna
- Acetylation
- Antibiotic resistance
- Automated data collection
- Cytoplasm
- Elongation factor
- Gtp-binding
- Membrane
- Methylation
- Nucleotide-binding
- Phosphoprotein
- Protein biosynthesis
- Protein translation
- Ribonucleoprotein
- Ribosomal protein
- Ribosomal protein/rna complex
- Rna-binding
- Rrna-binding
- Ternary complex
- Trna-binding