4V9D

Structures of the bacterial ribosome in classical and hybrid states of tRNA binding

This is a non-PDB format compatible entry.

Replaces:  3R8NReplaces:  3R8O

Summary for 4V9D

• Entry DOI: 10.2210/pdb4v9d/pdb
• Descriptor: 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (60 entities in total)
• Functional Keywords: protein biosynthesis, rna, trna, transfer rna, 30s, 70s, 16s, ribosomal subunit, ribosome recycling factor, rrf, ribosome
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A805
• Total number of polymer chains: 109
• Total formula weight: 4322347.90

Authors

Dunkle, J.A.,Wang, L.,Feldman, M.B.,Pulk, A.,Chen, V.B.,Kapral, G.J.,Noeske, J.,Richardson, J.S.,Blanchard, S.C.,Cate, J.H.D. (deposition date: 2012-07-31, release date: 2014-07-09, Last modification date: 2023-09-20)

Primary citation

Dunkle, J.A.,Wang, L.,Feldman, M.B.,Pulk, A.,Chen, V.B.,Kapral, G.J.,Noeske, J.,Richardson, J.S.,Blanchard, S.C.,Cate, J.H.
Structures of the bacterial ribosome in classical and hybrid states of tRNA binding.
Science, 332:981-984, 2011

PubMed Abstract: During protein synthesis, the ribosome controls the movement of tRNA and mRNA by means of large-scale structural rearrangements. We describe structures of the intact bacterial ribosome from Escherichia coli that reveal how the ribosome binds tRNA in two functionally distinct states, determined to a resolution of ~3.2 angstroms by means of x-ray crystallography. One state positions tRNA in the peptidyl-tRNA binding site. The second, a fully rotated state, is stabilized by ribosome recycling factor and binds tRNA in a highly bent conformation in a hybrid peptidyl/exit site. The structures help to explain how the ratchet-like motion of the two ribosomal subunits contributes to the mechanisms of translocation, termination, and ribosome recycling.

PubMed: 21596992
DOI: 10.1126/science.1202692

Experimental method

X-RAY DIFFRACTION (3 Å)