1r2x: Difference between revisions

Revision as of 15:46, 21 February 2008

Coordinates of L11 with 58nts of 23S rRNA fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome

OverviewOverview

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.

About this StructureAbout this Structure

1R2X is a Single protein structure of sequence from Thermotoga maritima. 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

Page seeded by OCA on Thu Feb 21 14:46:26 2008

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

OCA

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-[[Image:1r2x.gif|left|200px]]<br /><applet load="1r2x" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1r2x.gif|left|200px]]<br /><applet load="1r2x" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1r2x" />
 '''Coordinates of L11 with 58nts of 23S rRNA fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome'''<br />
 ==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.
+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.
 ==About this Structure==
-R2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R2X OCA].
+R2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R2X OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Ehrenberg, M.]]
 [[Category: Frank, J.]]
-[[Category: Harvey, S.C.]]
+[[Category: Harvey, S C.]]
 [[Category: Li, W.]]
-[[Category: Nielsen, R.C.]]
+[[Category: Nielsen, R C.]]
 [[Category: Nissen, P.]]
 [[Category: Sengupta, J.]]
-[[Category: Stagg, S.M.]]
+[[Category: Stagg, S M.]]
 [[Category: Valle, M.]]
 [[Category: Zavialov, A.]]
@@ Line 26: / Line 26: @@
 [[Category: rna]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:13:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:26 2008''