2H5E

Crystal structure of E.coli polypeptide release factor RF3

Summary for 2H5E

• Entry DOI: 10.2210/pdb2h5e/pdb
• Descriptor: Peptide chain release factor RF-3, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: beta barrel, translation
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 120190.27

Authors

Song, H.W.,Zhou, Z.H. (deposition date: 2006-05-26, release date: 2007-05-15, Last modification date: 2024-03-13)

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

X-RAY DIFFRACTION (2.8 Å)