2o0f: Difference between revisions

Revision as of 19:13, 21 February 2008

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

OverviewOverview

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.

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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OCA

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: ribosome]]
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