5IMR

Structure of ribosome bound to cofactor at 5.7 angstrom resolution

This is a non-PDB format compatible entry.

Summary for 5IMR

• Entry DOI: 10.2210/pdb5imr/pdb
• Related: 5IMQ
• EMDB information: 6585
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (57 entities in total)
• Functional Keywords: ef4/lepa, ribosome, translational gtpase factors, translocation, reverse
• Biological source: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); More
• Total number of polymer chains: 56
• Total formula weight: 2310421.33

Authors

Kumar, V.,Ero, R.,Jian, G.K.,Ahmed, T.,Zhan, Y.,Bhushan, S.,Gao, Y.G. (deposition date: 2016-03-06, release date: 2016-05-18, Last modification date: 2024-10-09)

Primary citation

Kumar, V.,Ero, R.,Ahmed, T.,Goh, K.J.,Zhan, Y.,Bhushan, S.,Gao, Y.G.
Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome
J.Biol.Chem., 291:12943-12950, 2016

PubMed Abstract: Elongation factor 4 (EF4) is a member of the family of ribosome-dependent translational GTPase factors, along with elongation factor G and BPI-inducible protein A. Although EF4 is highly conserved in bacterial, mitochondrial, and chloroplast genomes, its exact biological function remains controversial. Here we present the cryo-EM reconstitution of the GTP form of EF4 bound to the ribosome with P and E site tRNAs at 3.8-Å resolution. Interestingly, our structure reveals an unrotated ribosome rather than a clockwise-rotated ribosome, as observed in the presence of EF4-GDP and P site tRNA. In addition, we also observed a counterclockwise-rotated form of the above complex at 5.7-Å resolution. Taken together, our results shed light on the interactions formed between EF4, the ribosome, and the P site tRNA and illuminate the GTPase activation mechanism at previously unresolved detail.

PubMed: 27137929
DOI: 10.1074/jbc.M116.725945

Experimental method

ELECTRON MICROSCOPY (5.7 Å)