1QZC
Coordinates of S12, SH44, LH69 and SRL separately fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome
Summary for 1QZC
Entry DOI | 10.2210/pdb1qzc/pdb |
Related | 1FFK 1IBM 1QZA 1QZB 1QZD 1R2W 1R2X |
EMDB information | 1056 |
Descriptor | 16S rRNA, 23S rRNA, 30S ribosomal protein S12, ... (4 entities in total) |
Functional Keywords | ribosomal protein, rrna, rna binding protein-rna complex, rna binding protein/rna |
Biological source | Escherichia coli More |
Total number of polymer chains | 4 |
Total formula weight | 44215.09 |
Authors | Valle, M.,Zavialov, A.,Li, W.,Stagg, S.M.,Sengupta, J.,Nielsen, R.C.,Nissen, P.,Harvey, S.C.,Ehrenberg, M.,Frank, J. (deposition date: 2003-09-16, release date: 2003-11-04, Last modification date: 2024-02-14) |
Primary citation | Valle, M.,Zavialov, A.,Li, W.,Stagg, S.M.,Sengupta, J.,Nielsen, R.C.,Nissen, P.,Harvey, S.C.,Ehrenberg, M.,Frank, J. Incorporation of Aminoacyl-tRNA into the Ribosome as seen by Cryo-electron Microscopy Nat.Struct.Biol., 10:899-906, 2003 Cited by PubMed Abstract: 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. PubMed: 14566331DOI: 10.1038/nsb1003 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (9 Å) |
Structure validation
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