3eq3
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | [[3eq3]] is a 9 chain structure of [[Ribosomal protein S12]] with sequence 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]. | + | [[3eq3]] is a 9 chain structure of [[Ribosomal protein L11]] and [[Ribosomal protein S12]] with sequence 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]. |
==See Also== | ==See Also== | ||
| - | *[[Ribosomal protein S12]] | + | *[[Ribosomal protein L11|Ribosomal protein L11]] |
| + | *[[Ribosomal protein S12|Ribosomal protein S12]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:019020518</ref><references group="xtra"/> |
[[Category: Escherichia coli k12]] | [[Category: Escherichia coli k12]] | ||
[[Category: Agirrezabala, X.]] | [[Category: Agirrezabala, X.]] | ||
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[[Category: Li, W.]] | [[Category: Li, W.]] | ||
[[Category: A/t-trna]] | [[Category: A/t-trna]] | ||
| - | [[Category: Acetylation]] | ||
[[Category: Antibiotic resistance]] | [[Category: Antibiotic resistance]] | ||
[[Category: Automated data collection]] | [[Category: Automated data collection]] | ||
| - | [[Category: Cytoplasm]] | ||
[[Category: Elongation factor]] | [[Category: Elongation factor]] | ||
[[Category: Gtp-binding]] | [[Category: Gtp-binding]] | ||
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[[Category: Ribonucleoprotein]] | [[Category: Ribonucleoprotein]] | ||
[[Category: Ribosomal protein]] | [[Category: Ribosomal protein]] | ||
| - | [[Category: Ribosomal protein | + | [[Category: Ribosomal protein-rna complex]] |
[[Category: Rna-binding]] | [[Category: Rna-binding]] | ||
[[Category: Rrna-binding]] | [[Category: Rrna-binding]] | ||
[[Category: Ternary complex]] | [[Category: Ternary complex]] | ||
[[Category: Trna-binding]] | [[Category: Trna-binding]] | ||
Revision as of 04:50, 30 May 2012
Contents |
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 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
- 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
Categories: Escherichia coli k12 | Agirrezabala, X. | Frank, J. | Li, W. | A/t-trna | Antibiotic resistance | Automated data collection | 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
