title: Structures of the bacterial ribosome in classical and hybrid states of tRNA binding.
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.
authors: Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.
authors: Jack A
authors: JA
authors: Dunkle
authors: Leyi
authors: L
authors: Wang
authors: Michael B
authors: MB
authors: Feldman
authors: Arto
authors: A
authors: Pulk
authors: Vincent B
authors: VB
authors: Chen
authors: Gary J
authors: GJ
authors: Kapral
authors: Jonas
authors: J
authors: Noeske
authors: Jane S
authors: JS
authors: Richardson
authors: Scott C
authors: SC
authors: Blanchard
authors: Jamie H Doudna
authors: JH
authors: Cate
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