2O0F

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

Summary for 2O0F

• Entry DOI: 10.2210/pdb2o0f/pdb
• Related: 2H5E
• EMDB information: 1302
• Descriptor: Peptide chain release factor 3 (1 entity in total)
• Functional Keywords: rf3, ribosome, cryo-em, translation
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 59651.93

Authors

Gao, H.,Zhou, Z.,Rawat, U.,Huang, C.,Bouakaz, L.,Wang, C.,Liu, Y.,Zavialov, A.,Gursky, R.,Sanyal, S.,Ehrenberg, M.,Frank, J.,Song, H. (deposition date: 2006-11-27, release date: 2007-07-24, Last modification date: 2023-12-27)

Primary citation

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.
RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors
Cell(Cambridge,Mass.), 129:929-941, 2007

PubMed Abstract: 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.

PubMed: 17540173
DOI: 10.1016/j.cell.2007.03.050

Experimental method

ELECTRON MICROSCOPY (15.5 Å)