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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5749
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pubmed:dateCreated |
2005-11-7
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pubmed:databankReference |
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pubmed:abstractText |
We describe two structures of the intact bacterial ribosome from Escherichia coli determined to a resolution of 3.5 angstroms by x-ray crystallography. These structures provide a detailed view of the interface between the small and large ribosomal subunits and the conformation of the peptidyl transferase center in the context of the intact ribosome. Differences between the two ribosomes reveal a high degree of flexibility between the head and the rest of the small subunit. Swiveling of the head of the small subunit observed in the present structures, coupled to the ratchet-like motion of the two subunits observed previously, suggests a mechanism for the final movements of messenger RNA (mRNA) and transfer RNAs (tRNAs) during translocation.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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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 |
4
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pubmed:volume |
310
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
827-34
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16272117-Binding Sites,
pubmed-meshheading:16272117-Crystallization,
pubmed-meshheading:16272117-Crystallography, X-Ray,
pubmed-meshheading:16272117-Escherichia coli,
pubmed-meshheading:16272117-Escherichia coli Proteins,
pubmed-meshheading:16272117-Hydrogen Bonding,
pubmed-meshheading:16272117-Magnesium,
pubmed-meshheading:16272117-Models, Molecular,
pubmed-meshheading:16272117-Nucleic Acid Conformation,
pubmed-meshheading:16272117-Peptidyl Transferases,
pubmed-meshheading:16272117-Protein Biosynthesis,
pubmed-meshheading:16272117-Protein Conformation,
pubmed-meshheading:16272117-RNA, Bacterial,
pubmed-meshheading:16272117-RNA, Messenger,
pubmed-meshheading:16272117-RNA, Ribosomal,
pubmed-meshheading:16272117-RNA, Transfer,
pubmed-meshheading:16272117-Ribosomal Proteins,
pubmed-meshheading:16272117-Ribosomes
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pubmed:year |
2005
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pubmed:articleTitle |
Structures of the bacterial ribosome at 3.5 A resolution.
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pubmed:affiliation |
Department of Chemistry, University of California, Berkeley, CA 94720, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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