1qzc: Difference between revisions

Revision as of 06:41, 29 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:1qzc.png

Template:STRUCTURE 1qzc

Coordinates of S12, SH44, LH69 and SRL separately fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosomeCoordinates of S12, SH44, LH69 and SRL separately fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome

Template:ABSTRACT PUBMED 14566331

About this StructureAbout this Structure

1QZC is a Single protein structure of sequence from Escherichia coli and Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy., Valle M, Zavialov A, Li W, Stagg SM, Sengupta J, Nielsen RC, Nissen P, Harvey SC, Ehrenberg M, Frank J, Nat Struct Biol. 2003 Nov;10(11):899-906. Epub 2003 Oct 19. PMID:14566331

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

OCA

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-'''Coordinates of S12, SH44, LH69 and SRL separately fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome'''
+===Coordinates of S12, SH44, LH69 and SRL separately fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome===
-==Overview==
+<!--
-Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the ternary complex of aa-tRNA, elongation factor Tu (EF-Tu) and GTP. Here, we present a cryo-electron microscopy (cryo-EM) study, at a resolution of approximately 9 A, showing that during the incorporation of the aa-tRNA into the 70S ribosome of Escherichia coli, the flexibility of aa-tRNA allows the initial codon recognition and its accommodation into the ribosomal A site. In addition, a conformational change observed in the GTPase-associated center (GAC) of the ribosomal 50S subunit may provide the mechanism by which the ribosome promotes a relative movement of the aa-tRNA with respect to EF-Tu. This relative rearrangement seems to facilitate codon recognition by the incoming aa-tRNA, and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu. From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome.
+The line below this paragraph, {{ABSTRACT_PUBMED_14566331}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14566331 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14566331}}
 ==About this Structure==
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 [[Category: Ribosomal protein]]
 [[Category: Rrna]]
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