Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy.
Journal, issue, pages	Nat Struct Biol, Vol. 10, Issue 11, Page 899-906, Year 2003
Publish date	Oct 19, 2003
Authors	Mikel Valle / Andrey Zavialov / Wen Li / Scott M Stagg / Jayati Sengupta / Rikke C Nielsen / Poul Nissen / Stephen C Harvey / Måns Ehrenberg / Joachim Frank /
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, ...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.
External links	Nat Struct Biol / PubMed:14566331
Methods	EM (single particle)
Resolution	9.0 - 12.8 Å
Structure data	1055 1qza 1qzd 1r2x EMDB-1055: Locking and unlocking of ribosomal motions. PDB-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 PDB-1qzd: EF-Tu.kirromycin coordinates fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome PDB-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 Method: EM (single particle) / Resolution: 9.0 Å 1056 1qzb 1qzc 1r2w EMDB-1056: Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy. PDB-1qzb: Coordinates of the A-site tRNA model fitted into the cryo-EM map of 70S ribosome in the pre-translocational state PDB-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 PDB-1r2w: Coordinates of L11 with 58nts of 23S rRNA fitted into the cryo-EM map of the 70S ribosome Method: EM (single particle) / Resolution: 9.0 Å EMDB-1395: Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy. Method: EM (single particle) / Resolution: 12.8 Å
Source	escherichia coli (E. coli) thermus thermophilus (bacteria) thermotoga maritima (bacteria)
Keywords	RNA / tRNA model / decoding / A/T-site tRNA. / A-site tRNA / RNA Binding Protein/RNA / ribosomal protein / rRNA / RNA Binding Protein-RNA COMPLEX / BIOSYNTHETIC PROTEIN / Elongation factor