Structural highlights
4v9d is a 20 chain structure with sequence from Escherichia coli K-12. This structure supersedes the now removed PDB entries 3r8s, 3r8t, 4gd1, 4gd2, 3r8n and 3r8o. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Method: | X-ray diffraction, Resolution 3Å |
Ligands: | , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
RS2_ECOLI
Publication Abstract from PubMed
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.
Structures of the bacterial ribosome in classical and hybrid states of tRNA binding.,Dunkle JA, Wang L, Feldman MB, Pulk A, Chen VB, Kapral GJ, Noeske J, Richardson JS, Blanchard SC, Cate JH Science. 2011 May 20;332(6032):981-4. PMID:21596992[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dunkle JA, Wang L, Feldman MB, Pulk A, Chen VB, Kapral GJ, Noeske J, Richardson JS, Blanchard SC, Cate JH. Structures of the bacterial ribosome in classical and hybrid states of tRNA binding. Science. 2011 May 20;332(6032):981-4. PMID:21596992 doi:10.1126/science.1202692