rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6032
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pubmed:dateCreated |
2011-5-20
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/CA92584,
http://linkedlifedata.com/resource/pubmed/grant/GM074127-04S1,
http://linkedlifedata.com/resource/pubmed/grant/GM07739,
http://linkedlifedata.com/resource/pubmed/grant/GM079238,
http://linkedlifedata.com/resource/pubmed/grant/GM088674,
http://linkedlifedata.com/resource/pubmed/grant/GM65050,
http://linkedlifedata.com/resource/pubmed/grant/P01 GM063210-100005,
http://linkedlifedata.com/resource/pubmed/grant/P01-GM63210,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM065050-11,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM074127-04S1,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM088674-02,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM088674-03,
http://linkedlifedata.com/resource/pubmed/grant/RR-15301
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anticodon,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, 16S,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal, 23S,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Phe,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ribosome releasing factor,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, peptidyl-
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
20
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pubmed:volume |
332
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
981-4
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:21596992-Anticodon,
pubmed-meshheading:21596992-Crystallography, X-Ray,
pubmed-meshheading:21596992-Escherichia coli,
pubmed-meshheading:21596992-Escherichia coli Proteins,
pubmed-meshheading:21596992-Models, Molecular,
pubmed-meshheading:21596992-Nucleic Acid Conformation,
pubmed-meshheading:21596992-Protein Biosynthesis,
pubmed-meshheading:21596992-RNA, Bacterial,
pubmed-meshheading:21596992-RNA, Messenger,
pubmed-meshheading:21596992-RNA, Ribosomal, 16S,
pubmed-meshheading:21596992-RNA, Ribosomal, 23S,
pubmed-meshheading:21596992-RNA, Transfer, Amino Acyl,
pubmed-meshheading:21596992-RNA, Transfer, Phe,
pubmed-meshheading:21596992-Ribosomal Proteins,
pubmed-meshheading:21596992-Ribosome Subunits, Large, Bacterial,
pubmed-meshheading:21596992-Ribosome Subunits, Small, Bacterial
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pubmed:year |
2011
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pubmed:articleTitle |
Structures of the bacterial ribosome in classical and hybrid states of tRNA binding.
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pubmed:affiliation |
Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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