Structures of the Bacterial Ribosome in Classical and Hybrid States of tRNA Binding

被引：291

作者：

Dunkle, Jack A. ^{[1
,2
]}

Wang, Leyi ^{[3
]}

Feldman, Michael B. ^{[3
,4
]}

Pulk, Arto ^{[1
,2
]}

Chen, Vincent B. ^{[5
]}

Kapral, Gary J. ^{[5
]}

Noeske, Jonas ^{[1
,2
]}

Richardson, Jane S. ^{[5
]}

Blanchard, Scott C. ^{[3
]}

Cate, Jamie H. Doudna ^{[1
,2
,6
]}

机构：

[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA

[3] Cornell Univ, Weill Cornell Med Coll, Dept Physiol & Biophys, New York, NY 10065 USA

[4] Weill Cornell Rockefeller Univ Sloan Kettering Tr, New York, NY 10065 USA

[5] Duke Univ, Med Ctr, Dept Biochem, Durham, NC 27710 USA

[6] Univ Calif Berkeley, Lawrence Berkeley Lab, Phys Biosci Div, Berkeley, CA 94720 USA

来源：

SCIENCE | 2011年 / 332卷 / 6032期

基金：

美国国家卫生研究院;

关键词：

AMINOACYL-TRANSFER-RNA; CRYSTAL-STRUCTURE; RECYCLING FACTOR; INTERMEDIATE STATES; MESSENGER-RNA; 70S RIBOSOME; TRANSLOCATION; DYNAMICS; SITE; TRANSLATION;

D O I：

10.1126/science.1202692

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 similar to 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.

引用

页码：981 / 984

页数：4

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