3J9Z

Activation of GTP Hydrolysis in mRNA-tRNA Translocation by Elongation Factor G

This is a non-PDB format compatible entry.

Summary for 3J9Z

• Entry DOI: 10.2210/pdb3j9z/pdb
• Related: 3JA1
• EMDB information: 6315 6316
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S16, 30S ribosomal protein S17, ... (59 entities in total)
• Functional Keywords: 70s ribosome, elongation factor g, ef-g, ribosome
• Biological source: Escherichia coli; More
• Total number of polymer chains: 58
• Total formula weight: 2319879.16

Authors

Li, W.,Liu, Z.,Koripella, R.K.,Langlois, R.,Sanyal, S.,Frank, J. (deposition date: 2015-03-27, release date: 2015-07-01, Last modification date: 2024-02-21)

Primary citation

Li, W.,Liu, Z.,Koripella, R.K.,Langlois, R.,Sanyal, S.,Frank, J.
Activation of GTP hydrolysis in mRNA-tRNA translocation by elongation factor G.
Sci Adv, 1:e1500169-e1500169, 2015

PubMed Abstract: During protein synthesis, elongation of the polypeptide chain by each amino acid is followed by a translocation step in which mRNA and transfer RNA (tRNA) are advanced by one codon. This crucial step is catalyzed by elongation factor G (EF-G), a guanosine triphosphatase (GTPase), and accompanied by a rotation between the two ribosomal subunits. A mutant of EF-G, H91A, renders the factor impaired in guanosine triphosphate (GTP) hydrolysis and thereby stabilizes it on the ribosome. We use cryogenic electron microscopy (cryo-EM) at near-atomic resolution to investigate two complexes formed by EF-G H91A in its GTP state with the ribosome, distinguished by the presence or absence of the intersubunit rotation. Comparison of these two structures argues in favor of a direct role of the conserved histidine in the switch II loop of EF-G in GTPase activation, and explains why GTP hydrolysis cannot proceed with EF-G bound to the unrotated form of the ribosome.

PubMed: 26229983
DOI: 10.1126/sciadv.1500169

Experimental method

ELECTRON MICROSCOPY (3.6 Å)