4V9H

Crystal structure of the ribosome bound to elongation factor G in the guanosine triphosphatase state

This is a non-PDB format compatible entry.

Summary for 4V9H

• Entry DOI: 10.2210/pdb4v9h/pdb
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S16, 30S ribosomal protein S17, ... (61 entities in total)
• Functional Keywords: bacterial proteins, catalysis, models, molecular, peptide elongation factor g, protein biosynthesis, protein conformation, protein structure, tertiary, rna, bacterial, messenger, transfer, ribosomes, thermus thermophilus, ribosome, hybrid state, guanosine triphosphate, guanosine triphosphatase
• Biological source: Thermus thermophilus; More
• Cellular location: Cytoplasm: P80374
• Total number of polymer chains: 58
• Total formula weight: 2306027.96

Authors

Tourigny, D.S.,Fernandez, I.S.,Kelley, A.C.,Ramakrishnan, V. (deposition date: 2013-03-25, release date: 2014-07-09, Last modification date: 2014-12-10)

Primary citation

Tourigny, D.S.,Fernandez, I.S.,Kelley, A.C.,Ramakrishnan, V.
Elongation factor G bound to the ribosome in an intermediate state of translocation.
Science, 340:1235490-1235490, 2013

PubMed Abstract: A key step of translation by the ribosome is translocation, which involves the movement of messenger RNA (mRNA) and transfer RNA (tRNA) with respect to the ribosome. This allows a new round of protein chain elongation by placing the next mRNA codon in the A site of the 30S subunit. Translocation proceeds through an intermediate state in which the acceptor ends of the tRNAs have moved with respect to the 50S subunit but not the 30S subunit, to form hybrid states. The guanosine triphosphatase (GTPase) elongation factor G (EF-G) catalyzes the subsequent movement of mRNA and tRNA with respect to the 30S subunit. Here, we present a crystal structure at 3 angstrom resolution of the Thermus thermophilus ribosome with a tRNA in the hybrid P/E state bound to EF-G with a GTP analog. The structure provides insights into structural changes that facilitate translocation and suggests a common GTPase mechanism for EF-G and elongation factor Tu.

PubMed: 23812720
DOI: 10.1126/science.1235490

Experimental method

X-RAY DIFFRACTION (2.857 Å)