2rdo: Difference between revisions

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


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{{STRUCTURE_2rdo|  PDB=2rdo  |  SCENE=  }}  
{{STRUCTURE_2rdo|  PDB=2rdo  |  SCENE=  }}  


'''50S subunit with EF-G(GDPNP) and RRF bound'''
===50S subunit with EF-G(GDPNP) and RRF bound===




==Overview==
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After termination of protein synthesis, the bacterial ribosome is split into its 30S and 50S subunits by the action of ribosome recycling factor (RRF) and elongation factor G (EF-G) in a guanosine 5'-triphosphate (GTP)-hydrolysis-dependent manner. Based on a previous cryo-electron microscopy study of ribosomal complexes, we have proposed that the binding of EF-G to an RRF-containing posttermination ribosome triggers an interdomain rotation of RRF, which destabilizes two strong intersubunit bridges (B2a and B3) and, ultimately, separates the two subunits. Here, we present a 9-A (Fourier shell correlation cutoff of 0.5) cryo-electron microscopy map of a 50S x EF-G x guanosine 5'-[(betagamma)-imido]triphosphate x RRF complex and a quasi-atomic model derived from it, showing the interaction between EF-G and RRF on the 50S subunit in the presence of the noncleavable GTP analogue guanosine 5'-[(betagamma)-imido]triphosphate. The detailed information in this model and a comparative analysis of EF-G structures in various nucleotide- and ribosome-bound states show how rotation of the RRF head domain may be triggered by various domains of EF-G. For validation of our structural model, all known mutations in EF-G and RRF that relate to ribosome recycling have been taken into account. More importantly, our results indicate a substantial conformational change in the Switch I region of EF-G, suggesting that a conformational signal transduction mechanism, similar to that employed in transfer RNA translocation on the ribosome by EF-G, translates a large-scale movement of EF-G's domain IV, induced by GTP hydrolysis, into the domain rotation of RRF that eventually splits the ribosome into subunits.
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{{ABSTRACT_PUBMED_17996252}}


==About this Structure==
==About this Structure==
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[[Category: Trna-binding]]
[[Category: Trna-binding]]
[[Category: Zinc]]
[[Category: Zinc]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 16:41:56 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:37:08 2008''

Revision as of 04:37, 29 July 2008

File:2rdo.png

Template:STRUCTURE 2rdo

50S subunit with EF-G(GDPNP) and RRF bound

Template:ABSTRACT PUBMED 17996252

About this Structure

2RDO is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Specific interaction between EF-G and RRF and its implication for GTP-dependent ribosome splitting into subunits., Gao N, Zavialov AV, Ehrenberg M, Frank J, J Mol Biol. 2007 Dec 14;374(5):1345-58. Epub 2007 Oct 16. PMID:17996252

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