1ZN0

Coordinates of RRF and EF-G fitted into Cryo-EM map of the 50S subunit bound with both EF-G (GDPNP) and RRF

Summary for 1ZN0

• Entry DOI: 10.2210/pdb1zn0/pdb
• Related: 1EK8 1P6G 1PN6
• EMDB information: 1127 1128
• Descriptor: 16S RIBOSOMAL RNA, Ribosome recycling factor, ELONGATION FACTOR G (3 entities in total)
• Functional Keywords: ribosome recycling factor, elongation factor g, 50s subunit, translation-biosynthetic protein-rna complex, translation/biosynthetic protein/rna
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A805
• Total number of polymer chains: 3
• Total formula weight: 106581.76

Authors

Gao, N.,Zavialov, A.V.,Li, W.,Sengupta, J.,Valle, M.,Gursky, R.P.,Ehrenberg, M.,Frank, J. (deposition date: 2005-05-11, release date: 2005-06-14, Last modification date: 2024-02-14)

Primary citation

Gao, N.,Zavialov, A.V.,Li, W.,Sengupta, J.,Valle, M.,Gursky, R.P.,Ehrenberg, M.,Frank, J.
Mechanism for the disassembly of the posttermination complex inferred from cryo-EM studies.
Mol.Cell, 18:663-674, 2005

PubMed Abstract: Ribosome recycling, the disassembly of the posttermination complex after each round of protein synthesis, is an essential step in mRNA translation, but its mechanism has remained obscure. In eubacteria, recycling is catalyzed by RRF (ribosome recycling factor) and EF-G (elongation factor G). By using cryo-electron microscopy, we have obtained two density maps, one of the RRF bound posttermination complex and one of the 50S subunit bound with both EF-G and RRF. Comparing the two maps, we found domain I of RRF to be in the same orientation, while domain II in the EF-G-containing 50S subunit is extensively rotated (approximately 60 degrees) compared to its orientation in the 70S complex. Mapping the 50S conformation of RRF onto the 70S posttermination complex suggests that it can disrupt the intersubunit bridges B2a and B3, and thus effect a separation of the two subunits. These observations provide the structural basis for the mechanism by which the posttermination complex is split into subunits by the joint action of RRF and EF-G.

PubMed: 15949441
DOI: 10.1016/j.molcel.2005.05.005

Experimental method

ELECTRON MICROSCOPY (15.5 Å)