4V5E

Insights into translational termination from the structure of RF2 bound to the ribosome

This is a non-PDB format compatible entry.

Replaces:  2JL5Replaces:  2JL6Replaces:  2JL7Replaces:  2JL8

Summary for 4V5E

• Entry DOI: 10.2210/pdb4v5e/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
• Descriptor: 16S ribosomal RNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (61 entities in total)
• Functional Keywords: ribosomal protein, ribonucleoprotein, termination, rrna-binding, trna-binding, metal-binding, rf2, trna, mrna, ribosome, protein biosynthesis, zinc-finger, rna-binding, translation
• Biological source: Escherichia coli K-12; More
• Cellular location: Cytoplasm : Q5SM01
• Total number of polymer chains: 118
• Total formula weight: 4640998.44

Authors

Weixlbaumer, A.,Jin, H.,Neubauer, C.,Voorhees, R.M.,Petry, S.,Kelley, A.C.,Ramakrishnan, V. (deposition date: 2009-04-30, release date: 2014-07-09, Last modification date: 2024-11-20)

Primary citation

Weixlbaumer, A.,Jin, H.,Neubauer, C.,Voorhees, R.M.,Petry, S.,Kelley, A.C.,Ramakrishnan, V.
Insights Into Translational Termination from the Structure of Rf2 Bound to the Ribosome.
Science, 322:953-956, 2008

PubMed Abstract: The termination of protein synthesis occurs through the specific recognition of a stop codon in the A site of the ribosome by a release factor (RF), which then catalyzes the hydrolysis of the nascent protein chain from the P-site transfer RNA. Here we present, at a resolution of 3.5 angstroms, the crystal structure of RF2 in complex with its cognate UGA stop codon in the 70S ribosome. The structure provides insight into how RF2 specifically recognizes the stop codon; it also suggests a model for the role of a universally conserved GGQ motif in the catalysis of peptide release.

PubMed: 18988853
DOI: 10.1126/science.1164840

Experimental method

X-RAY DIFFRACTION (3.45 Å)