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1qza
From Proteopedia
(New page: 200px<br /><applet load="1qza" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qza" /> '''Coordinates of the A/T site tRNA model fitte...) |
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| - | [[Image:1qza.gif|left|200px]]<br /><applet load="1qza" size=" | + | [[Image:1qza.gif|left|200px]]<br /><applet load="1qza" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qza" /> | caption="1qza" /> | ||
'''Coordinates of the A/T site tRNA model fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome'''<br /> | '''Coordinates of the A/T site tRNA model fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the | + | 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== | ==About this Structure== | ||
| - | 1QZA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1QZA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ehrenberg, M.]] | [[Category: Ehrenberg, M.]] | ||
[[Category: Frank, J.]] | [[Category: Frank, J.]] | ||
| - | [[Category: Harvey, S | + | [[Category: Harvey, S C.]] |
[[Category: Li, W.]] | [[Category: Li, W.]] | ||
| - | [[Category: Nielsen, R | + | [[Category: Nielsen, R C.]] |
[[Category: Nissen, P.]] | [[Category: Nissen, P.]] | ||
[[Category: Sengupta, J.]] | [[Category: Sengupta, J.]] | ||
| - | [[Category: Stagg, S | + | [[Category: Stagg, S M.]] |
[[Category: Valle, M.]] | [[Category: Valle, M.]] | ||
[[Category: Zavialov, A.]] | [[Category: Zavialov, A.]] | ||
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[[Category: trna model]] | [[Category: trna model]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:22 2008'' |
Revision as of 12:45, 21 February 2008
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Coordinates of the A/T site tRNA model 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.
About this Structure
1QZA is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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 14:45:22 2008
Categories: Protein complex | Ehrenberg, M. | Frank, J. | Harvey, S C. | Li, W. | Nielsen, R C. | Nissen, P. | Sengupta, J. | Stagg, S M. | Valle, M. | Zavialov, A. | A/t-site trna. | Decoding | Trna model
