3ep2: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 8: Line 8:


==About this Structure==
==About this Structure==
[[3ep2]] 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=3EP2 OCA].  
[[3ep2]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EP2 OCA].  


==See Also==
==See Also==
Line 16: Line 16:
==Reference==
==Reference==
<ref group="xtra">PMID:019020518</ref><references group="xtra"/>
<ref group="xtra">PMID:019020518</ref><references group="xtra"/>
[[Category: Escherichia coli k12]]
[[Category: Escherichia coli k-12]]
[[Category: Agirrezabala, X.]]
[[Category: Agirrezabala, X.]]
[[Category: Frank, J.]]
[[Category: Frank, J.]]

Revision as of 20:32, 20 October 2012


PDB ID 3ep2

Drag the structure with the mouse to rotate
3ep2, resolution 9.00Å ()
Related: 2avy, 2aw4, 1qza, 1ob2, 3eq3, 3eq4
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

Publication Abstract from PubMed

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 9 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1]

  1. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA