4V4R

Crystal structure of the whole ribosomal complex.

This is a non-PDB format compatible entry.

Summary for 4V4R

• Entry DOI: 10.2210/pdb4v4r/pdb
• Related: 2B66 2B9M 2B9N 2B9O 2B9P
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S7, 30S ribosomal protein S8, ... (56 entities in total)
• Functional Keywords: ribosome, translation, release factor
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm : P96077
• Total number of polymer chains: 56
• Total formula weight: 2277812.16

Authors

Petry, S.,Brodersen, D.E.,Murphy IV, F.V.,Dunham, C.M.,Selmer, M.,Tarry, M.J.,Kelley, A.C.,Ramakrishnan, V. (deposition date: 2005-09-30, release date: 2014-07-09, Last modification date: 2024-12-25)

Primary citation

Petry, S.,Brodersen, D.E.,Murphy IV, F.V.,Dunham, C.M.,Selmer, M.,Tarry, M.J.,Kelley, A.C.,Ramakrishnan, V.
Crystal Structures of the Ribosome in Complex with Release Factors RF1 and RF2 Bound to a Cognate Stop Codon.
Cell(Cambridge,Mass.), 123:1255-1266, 2005

PubMed Abstract: During protein synthesis, translational release factors catalyze the release of the polypeptide chain when a stop codon on the mRNA reaches the A site of the ribosome. The detailed mechanism of this process is currently unknown. We present here the crystal structures of the ribosome from Thermus thermophilus with RF1 and RF2 bound to their cognate stop codons, at resolutions of 5.9 Angstrom and 6.7 Angstrom, respectively. The structures reveal details of interactions of the factors with the ribosome and mRNA, including elements previously implicated in decoding and peptide release. They also shed light on conformational changes both in the factors and in the ribosome during termination. Differences seen in the interaction of RF1 and RF2 with the L11 region of the ribosome allow us to rationalize previous biochemical data. Finally, this work demonstrates the feasibility of crystallizing ribosomes with bound factors at a defined state along the translational pathway.

PubMed: 16377566
DOI: 10.1016/j.cell.2005.09.039

Experimental method

X-RAY DIFFRACTION (5.9 Å)