2o0f: Difference between revisions

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{{STRUCTURE_2o0f|  PDB=2o0f  |  SCENE=  }}  
{{STRUCTURE_2o0f|  PDB=2o0f  |  SCENE=  }}  


'''Docking of the modified RF3 X-ray structure into cryo-EM map of E.coli 70S ribosome bound with RF3'''
===Docking of the modified RF3 X-ray structure into cryo-EM map of E.coli 70S ribosome bound with RF3===




==Overview==
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During translation termination, class II release factor RF3 binds to the ribosome to promote rapid dissociation of a class I release factor (RF) in a GTP-dependent manner. We present the crystal structure of E. coli RF3*GDP, which has a three-domain architecture strikingly similar to the structure of EF-Tu*GTP. Biochemical data on RF3 mutants show that a surface region involving domains II and III is important for distinct steps in the action cycle of RF3. Furthermore, we present a cryo-electron microscopy (cryo-EM) structure of the posttermination ribosome bound with RF3 in the GTP form. Our data show that RF3*GTP binding induces large conformational changes in the ribosome, which break the interactions of the class I RF with both the decoding center and the GTPase-associated center of the ribosome, apparently leading to the release of the class I RF.
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{{ABSTRACT_PUBMED_17540173}}


==About this Structure==
==About this Structure==
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[[Category: Rf3]]
[[Category: Rf3]]
[[Category: Ribosome]]
[[Category: Ribosome]]
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Revision as of 19:34, 28 July 2008

File:2o0f.png

Template:STRUCTURE 2o0f

Docking of the modified RF3 X-ray structure into cryo-EM map of E.coli 70S ribosome bound with RF3Docking of the modified RF3 X-ray structure into cryo-EM map of E.coli 70S ribosome bound with RF3

Template:ABSTRACT PUBMED 17540173

About this StructureAbout this Structure

2O0F is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors., Gao H, Zhou Z, Rawat U, Huang C, Bouakaz L, Wang C, Cheng Z, Liu Y, Zavialov A, Gursky R, Sanyal S, Ehrenberg M, Frank J, Song H, Cell. 2007 Jun 1;129(5):929-41. PMID:17540173

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