1qza
From Proteopedia
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|PDB= 1qza |SIZE=350|CAPTION= <scene name='initialview01'>1qza</scene> | |PDB= 1qza |SIZE=350|CAPTION= <scene name='initialview01'>1qza</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ob2|1OB2]], [[1qzb|1QZB]], [[1qzc|1QZC]], [[1qzd|1QZD]], [[1r2w|1R2W]], [[1r2x|1R2X]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qza OCA], [http://www.ebi.ac.uk/pdbsum/1qza PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qza RCSB]</span> | ||
}} | }} | ||
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[[Category: trna model]] | [[Category: trna model]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:21:04 2008'' |
Revision as of 20:21, 30 March 2008
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| Ligands: | , , , | ||||||
| Related: | 1OB2, 1QZB, 1QZC, 1QZD, 1R2W, 1R2X
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 23:21:04 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
