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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2006-5-22
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pubmed:databankReference |
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pubmed:abstractText |
The highly conserved ribonuclease RNase Z catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Here we present the structure of the complex between Bacillus subtilis RNase Z and tRNA(Thr), the first structure of a ribonucleolytic processing enzyme bound to tRNA. Binding of tRNA to RNase Z causes conformational changes in both partners to promote reorganization of the catalytic site and tRNA cleavage.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1545-9993
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
376-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16518398-Bacillus subtilis,
pubmed-meshheading:16518398-Catalytic Domain,
pubmed-meshheading:16518398-Endoribonucleases,
pubmed-meshheading:16518398-Macromolecular Substances,
pubmed-meshheading:16518398-Models, Molecular,
pubmed-meshheading:16518398-Nucleic Acid Conformation,
pubmed-meshheading:16518398-Protein Conformation,
pubmed-meshheading:16518398-RNA, Bacterial,
pubmed-meshheading:16518398-RNA, Transfer, Thr,
pubmed-meshheading:16518398-RNA Processing, Post-Transcriptional
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pubmed:year |
2006
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pubmed:articleTitle |
Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA.
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pubmed:affiliation |
Centre National de la Recherche (CNRS) FRC550, Institut de Biologie Physico-Chimique, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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