3ep2: Difference between revisions
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[[Image: | ==Model of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM== | ||
<StructureSection load='3ep2' size='340' side='right' caption='[[3ep2]], [[Resolution|resolution]] 9.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EP2 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2avy|2avy]], [[2aw4|2aw4]], [[1qza|1qza]], [[1ob2|1ob2]], [[3eq3|3eq3]], [[3eq4|3eq4]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ep2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ep2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ep2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ep2 PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ep/3ep2_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:19020518</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Elongation factor|Elongation factor]] | |||
*[[Ribosomal protein L11|Ribosomal protein L11]] | *[[Ribosomal protein L11|Ribosomal protein L11]] | ||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Agirrezabala, X.]] | [[Category: Agirrezabala, X.]] | ||
Revision as of 13:19, 29 September 2014
Model of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM
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Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Escherichia coli k-12
- 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
