4V9P

Control of ribosomal subunit rotation by elongation factor G

This is a non-PDB format compatible entry.

Summary for 4V9P

• Entry DOI: 10.2210/pdb4v9p/pdb
• Related PRD ID: PRD_000226
• Descriptor: 23S rRNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (59 entities in total)
• Functional Keywords: protein biosynthesis, ribosome, rna, ef-g, elongation, factor, gtp, gdpcp, viomycin, trna, tranlocation, exit, peptidyl, 50s, 70s, 23s, ribosomal subunit, ribosome-antibiotic complex, ribosome/antibiotic
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A6M8
• Total number of polymer chains: 217
• Total formula weight: 8915594.89

Authors

Pulk, A.,Cate, J.H.D. (deposition date: 2013-05-03, release date: 2014-07-09, Last modification date: 2014-12-17)

Primary citation

Pulk, A.,Cate, J.H.
Control of ribosomal subunit rotation by elongation factor G.
Science, 340:1235970-1235970, 2013

PubMed Abstract: Protein synthesis by the ribosome requires the translocation of transfer RNAs and messenger RNA by one codon after each peptide bond is formed, a reaction that requires ribosomal subunit rotation and is catalyzed by the guanosine triphosphatase (GTPase) elongation factor G (EF-G). We determined 3 angstrom resolution x-ray crystal structures of EF-G complexed with a nonhydrolyzable guanosine 5'-triphosphate (GTP) analog and bound to the Escherichia coli ribosome in different states of ribosomal subunit rotation. The structures reveal that EF-G binding to the ribosome stabilizes switch regions in the GTPase active site, resulting in a compact EF-G conformation that favors an intermediate state of ribosomal subunit rotation. These structures suggest that EF-G controls the translocation reaction by cycles of conformational rigidity and relaxation before and after GTP hydrolysis.

PubMed: 23812721
DOI: 10.1126/science.1235970

Experimental method

X-RAY DIFFRACTION (2.9 Å)