3eq3
From Proteopedia
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| + | {{STRUCTURE_3eq3| PDB=3eq3 | SCENE= }} | ||
| - | + | ===Model of tRNA(Trp)-EF-Tu in the ribosomal pre-accommodated state revealed by cryo-EM=== | |
| - | Description: Model of tRNA(Trp)-EF-Tu in the ribosomal pre-accommodated state revealed by cryo-EM | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | <!-- |
| + | The line below this paragraph, {{ABSTRACT_PUBMED_19020518}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 19020518 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_19020518}} | ||
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| + | ==About this Structure== | ||
| + | 3EQ3 is a 9 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli_k12 Escherichia coli k12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EQ3 OCA]. | ||
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| + | ==Reference== | ||
| + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/19020518 19020518] | ||
| + | [[Category: Escherichia coli k12]] | ||
| + | [[Category: Agirrezabala, X.]] | ||
| + | [[Category: Frank, J.]] | ||
| + | [[Category: Li, W.]] | ||
| + | [[Category: A/t-trna]] | ||
| + | [[Category: Acetylation]] | ||
| + | [[Category: Antibiotic resistance]] | ||
| + | [[Category: Automated data collection]] | ||
| + | [[Category: Cytoplasm]] | ||
| + | [[Category: Elongation factor]] | ||
| + | [[Category: Gtp-binding]] | ||
| + | [[Category: Membrane]] | ||
| + | [[Category: Methylation]] | ||
| + | [[Category: Nucleotide-binding]] | ||
| + | [[Category: Phosphoprotein]] | ||
| + | [[Category: Protein biosynthesis]] | ||
| + | [[Category: Protein translation]] | ||
| + | [[Category: Ribonucleoprotein]] | ||
| + | [[Category: Ribosomal protein]] | ||
| + | [[Category: Ribosomal protein/rna complex]] | ||
| + | [[Category: Rna-binding]] | ||
| + | [[Category: Rrna-binding]] | ||
| + | [[Category: Ternary complex]] | ||
| + | [[Category: Trna-binding]] | ||
| + | |||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 17 13:45:39 2008'' | ||
Revision as of 11:45, 17 December 2008
Model of tRNA(Trp)-EF-Tu 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 Structure
3EQ3 is a 9 chains structure of sequences from Escherichia coli k12. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Dec 17 13:45:39 2008
Categories: Escherichia coli k12 | Agirrezabala, X. | Frank, J. | Li, W. | 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
