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Structures of the bacterial ribosome in classical and hybrid states of tRNA binding.(REPORTS)(Author abstract)(Report)

Dunkle, Jack A. ; Wang, Leyi ; Feldman, Michael B. ; Pulk, Arto ; Chen, Vincent B. ; Kapral, Gary J. ; Noeske, Jonas ; Richardson, Jane S. ; Blanchard, Scott C. ; Cate, Jamie H. Doudna

Science, May 20, 2011, Vol.332(6032), p.981(4) [Tạp chí có phản biện]

ISSN: 0036-8075

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  • Nhan đề:
    Structures of the bacterial ribosome in classical and hybrid states of tRNA binding.(REPORTS)(Author abstract)(Report)
  • Tác giả: Dunkle, Jack A. ; Wang, Leyi ; Feldman, Michael B. ; Pulk, Arto ; Chen, Vincent B. ; Kapral, Gary J. ; Noeske, Jonas ; Richardson, Jane S. ; Blanchard, Scott C. ; Cate, Jamie H. Doudna
  • Chủ đề: Ribosomes -- Properties ; Transfer Rna -- Properties ; Protein Synthesis -- Physiological Aspects
  • Là 1 phần của: Science, May 20, 2011, Vol.332(6032), p.981(4)
  • Mô tả: 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. 10.1126/science.1202692
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0036-8075

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