4V5J

Structure of the 70S ribosome bound to Release factor 2 and a substrate analog provides insights into catalysis of peptide release

This is a non-PDB format compatible entry.

Summary for 4V5J

• Entry DOI: 10.2210/pdb4v5j/pdb
• Related: 1DV4 1EG0 1EMI 1FJG 1FKA 1G1X 1GIX 1HNW 1HNX 1HNZ 1HR0 1I94 1I95 1I96 1I97 1IBK 1IBL 1IBM 1J5E 1JGO 1JGP 1JGQ 1L1U 1N32 1N33 1N34 1N36 1PN7 1PN8 1PNS 1PNX 1QD7 1QZC 1RSS 1TWT 1VOV 1XMO 1XMQ 1XNQ 1XNR 1YL4 2B64 2B9M 2B9O 2F4V 2J00 2J02 2UU9 2UUA 2UUB 2UUC 2UXB 2UXC 2UXD 2V46 2V48 2VQE 2VQF 2WDG 2WDH 2WDK 2WDM 2WH1 2WH3 2WRN 2WRQ
• Descriptor: 16S Ribosomal RNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (61 entities in total)
• Functional Keywords: ribosomal protein, ribonucleoprotein, trna-binding, rrna-binding, metal-binding, ribosome, zinc-finger, translation
• Biological source: THERMUS THERMOPHILUS; More
• Cellular location: Cytoplasm : Q5SM01
• Total number of polymer chains: 118
• Total formula weight: 4650645.70

Authors

Jin, H.,Kelley, A.C.,Loakes, D.,Ramakrishnan, V. (deposition date: 2010-03-24, release date: 2014-07-09, Last modification date: 2024-01-10)

Primary citation

Jin, H.,Kelley, A.C.,Loakes, D.,Ramakrishnan, V.
Structure of the 70S ribosome bound to release factor 2 and a substrate analog provides insights into catalysis of peptide release.
Proc. Natl. Acad. Sci. U.S.A., 107:8593-8598, 2010

PubMed Abstract: We report the crystal structure of release factor 2 bound to ribosome with an aminoacyl tRNA substrate analog at the ribosomal P site, at 3.1 A resolution. The structure shows that upon stop-codon recognition, the universally conserved GGQ motif packs tightly into the peptidyl transferase center. Nucleotide A2602 of 23S rRNA, implicated in peptide release, packs with the GGQ motif in release factor 2. The ribose of A76 of the peptidyl-tRNA adopts the C2'-endo conformation, and the 2' hydroxyl of A76 is within hydrogen-bond distance of the 2' hydroxyl of A2451. The structure suggests how a catalytic water can be coordinated in the peptidyl transferase center and, together with previous biochemical and computational data, suggests a model for how the ester bond between the peptidyl tRNA and the nascent peptide is hydrolyzed.

PubMed: 20421507
DOI: 10.1073/pnas.1003995107

Experimental method

X-RAY DIFFRACTION (3.1 Å)