3eq3
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 3EQ3 is a | + | 3EQ3 is a [[Protein complex]] 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]. |
==Reference== | ==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] | 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: Escherichia coli k12]] | ||
| - | [[Category: | + | [[Category: Protein complex]] |
| - | [[Category: | + | [[Category: Pdbx_ordinal=, <PDBx:audit_author.]] |
| - | + | ||
[[Category: A/t-trna]] | [[Category: A/t-trna]] | ||
[[Category: Acetylation]] | [[Category: Acetylation]] | ||
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[[Category: Trna-binding]] | [[Category: Trna-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 7 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 7 20:11:52 2009'' |
Revision as of 17:42, 8 January 2009
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 Protein complex 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[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
Page seeded by OCA on Wed Jan 7 20:11:52 2009
Categories: 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
