1mj1
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(New page: 200px<br /><applet load="1mj1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mj1" /> '''FITTING THE TERNARY COMPLEX OF EF-Tu/tRNA/GT...)
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Revision as of 19:19, 20 November 2007
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FITTING THE TERNARY COMPLEX OF EF-Tu/tRNA/GTP AND RIBOSOMAL PROTEINS INTO A 13 A CRYO-EM MAP OF THE COLI 70S RIBOSOME
Overview
The mRNA codon in the ribosomal A-site is recognized by aminoacyl-tRNA, (aa-tRNA) in a ternary complex with elongation factor Tu (EF-Tu) and GTP., Here we report the 13 A resolution three-dimensional reconstruction, determined by cryo-electron microscopy of the kirromycin-stalled, codon-recognition complex. The structure of the ternary complex is, distorted by binding of the tRNA anticodon arm in the decoding center. The, aa-tRNA interacts with 16S rRNA, helix 69 of 23S rRNA and proteins S12 and, L11, while the sarcin-ricin loop of 23S rRNA contacts domain 1 of EF-Tu, near the nucleotide-binding pocket. These results provide a detailed, snapshot view of an important functional state of the ribosome and suggest, mechanisms of decoding and GTPase activation.
About this Structure
1MJ1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex., Stark H, Rodnina MV, Wieden HJ, Zemlin F, Wintermeyer W, van Heel M, Nat Struct Biol. 2002 Nov;9(11):849-54. PMID:12379845
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