2p8x: Difference between revisions

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[[Image:2p8x.jpg|left|200px]]
{{Seed}}
[[Image:2p8x.png|left|200px]]


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{{STRUCTURE_2p8x|  PDB=2p8x  |  SCENE=  }}  
{{STRUCTURE_2p8x|  PDB=2p8x  |  SCENE=  }}  


'''Fitted structure of ADPR-eEF2 in the 80S:ADPR-eEF2:GDPNP cryo-EM reconstruction'''
===Fitted structure of ADPR-eEF2 in the 80S:ADPR-eEF2:GDPNP cryo-EM reconstruction===




==Overview==
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On the basis of kinetic data on ribosome protein synthesis, the mechanical energy for translocation of the mRNA-tRNA complex is thought to be provided by GTP hydrolysis of an elongation factor (eEF2 in eukaryotes, EF-G in bacteria). We have obtained cryo-EM reconstructions of eukaryotic ribosomes complexed with ADP-ribosylated eEF2 (ADPR-eEF2), before and after GTP hydrolysis, providing a structural basis for analyzing the GTPase-coupled mechanism of translocation. Using the ADP-ribosyl group as a distinct marker, we observe conformational changes of ADPR-eEF2 that are due strictly to GTP hydrolysis. These movements are likely representative of native eEF2 motions in a physiological context and are sufficient to uncouple the mRNA-tRNA complex from two universally conserved bases in the ribosomal decoding center (A1492 and A1493 in Escherichia coli) during translocation. Interpretation of these data provides a detailed two-step model of translocation that begins with the eEF2/EF-G binding-induced ratcheting motion of the small ribosomal subunit. GTP hydrolysis then uncouples the mRNA-tRNA complex from the decoding center so translocation of the mRNA-tRNA moiety may be completed by a head rotation of the small subunit.
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{{ABSTRACT_PUBMED_17446867}}


==About this Structure==
==About this Structure==
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[[Category: Gtpase]]
[[Category: Gtpase]]
[[Category: Translocation]]
[[Category: Translocation]]
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