1rf8: Difference between revisions

Revision as of 10:52, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1rf8.png

Template:STRUCTURE 1rf8

Solution structure of the yeast translation initiation factor eIF4E in complex with m7GDP and eIF4GI residues 393 to 490Solution structure of the yeast translation initiation factor eIF4E in complex with m7GDP and eIF4GI residues 393 to 490

Template:ABSTRACT PUBMED 14675538

About this StructureAbout this Structure

1RF8 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full experimental information is available from OCA.

ReferenceReference

Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E., Gross JD, Moerke NJ, von der Haar T, Lugovskoy AA, Sachs AB, McCarthy JE, Wagner G, Cell. 2003 Dec 12;115(6):739-50. PMID:14675538

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-[[Image:1rf8.gif|left|200px]]
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 {{STRUCTURE_1rf8|  PDB=1rf8  |  SCENE=  }}
-'''Solution structure of the yeast translation initiation factor eIF4E in complex with m7GDP and eIF4GI residues 393 to 490'''
+===Solution structure of the yeast translation initiation factor eIF4E in complex with m7GDP and eIF4GI residues 393 to 490===
-==Overview==
+<!--
-The eukaryotic initiation factor 4G (eIF4G) is the core of a multicomponent switch controlling gene expression at the level of translation initiation. It interacts with the small ribosomal subunit interacting protein, eIF3, and the eIF4E/cap-mRNA complex in order to load the ribosome onto mRNA during cap-dependent translation. We describe the solution structure of the complex between yeast eIF4E/cap and eIF4G (393-490). Binding triggers a coupled folding transition of eIF4G (393-490) and the eIF4E N terminus resulting in a molecular bracelet whereby eIF4G (393-490) forms a right-handed helical ring that wraps around the N terminus of eIF4E. Cofolding allosterically enhances association of eIF4E with the cap and is required for maintenance of optimal growth and polysome distributions in vivo. Our data explain how mRNA, eIF4E, and eIF4G exists as a stable mRNP that may facilitate multiple rounds of ribosomal loading during translation initiation, a key determinant in the overall rate of protein synthesis.
+The line below this paragraph, {{ABSTRACT_PUBMED_14675538}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14675538 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14675538}}
 ==About this Structure==
-RF8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RF8 OCA].
+RF8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RF8 OCA].
 ==Reference==
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 [[Category: Protein biosynthesis]]
 [[Category: Translation regulation]]
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