4V63

Structural basis for translation termination on the 70S ribosome.

This is a non-PDB format compatible entry.

Summary for 4V63

• Entry DOI: 10.2210/pdb4v63/pdb
• Related: 3D5B 3D5C 3D5D
• Descriptor: 16S RRNA, 30S ribosomal protein S8, 30S ribosomal protein S9, ... (57 entities in total)
• Functional Keywords: ribosome, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, metal-binding, zinc-finger, trna-binding, protein biosynthesis
• Biological source: Thermus thermophilus; More
• Cellular location: Cytoplasm : Q72HB8
• Total number of polymer chains: 112
• Total formula weight: 4627220.30

Authors

Laurberg, M.,Asahara, H.,Korostelev, A.,Zhu, J.,Trakhanov, S.,Noller, H.F. (deposition date: 2008-05-16, release date: 2014-07-09, Last modification date: 2024-11-20)

Primary citation

Laurberg, M.,Asahara, H.,Korostelev, A.,Zhu, J.,Trakhanov, S.,Noller, H.F.
Structural basis for translation termination on the 70S ribosome
Nature, 454:852-857, 2008

PubMed Abstract: At termination of protein synthesis, type I release factors promote hydrolysis of the peptidyl-transfer RNA linkage in response to recognition of a stop codon. Here we describe the crystal structure of the Thermus thermophilus 70S ribosome in complex with the release factor RF1, tRNA and a messenger RNA containing a UAA stop codon, at 3.2 A resolution. The stop codon is recognized in a pocket formed by conserved elements of RF1, including its PxT recognition motif, and 16S ribosomal RNA. The codon and the 30S subunit A site undergo an induced fit that results in stabilization of a conformation of RF1 that promotes its interaction with the peptidyl transferase centre. Unexpectedly, the main-chain amide group of Gln 230 in the universally conserved GGQ motif of the factor is positioned to contribute directly to peptidyl-tRNA hydrolysis.

PubMed: 18596689
DOI: 10.1038/nature07115

Experimental method

X-RAY DIFFRACTION (3.207 Å)