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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 |
2003-4-29
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pubmed:databankReference |
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pubmed:abstractText |
A structure of the Escherichia coli chromosomal MazE/MazF addiction module has been determined at 1.7 A resolution. Addiction modules consist of stable toxin and unstable antidote proteins that govern bacterial cell death. MazE (antidote) and MazF (toxin) form a linear heterohexamer composed of alternating toxin and antidote homodimers (MazF(2)-MazE(2)-MazF(2)). The MazE homodimer contains a beta barrel from which two extended C termini project, making interactions with flanking MazF homodimers that resemble the plasmid-encoded toxins CcdB and Kid. The MazE/MazF heterohexamer structure documents that the mechanism of antidote-toxin recognition is common to both chromosomal and plasmid-borne addiction modules, and provides general molecular insights into toxin function, antidote degradation in the absence of toxin, and promoter DNA binding by antidote/toxin complexes.
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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/Antidotes,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/CcdB protein, Plasmid F,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/MazE protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/MazF protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/kid toxin protein, E coli plasmid R1
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
875-84
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12718874-Antidotes,
pubmed-meshheading:12718874-Bacterial Proteins,
pubmed-meshheading:12718874-Bacterial Toxins,
pubmed-meshheading:12718874-Cell Death,
pubmed-meshheading:12718874-Chromosomes, Bacterial,
pubmed-meshheading:12718874-DNA-Binding Proteins,
pubmed-meshheading:12718874-Endoribonucleases,
pubmed-meshheading:12718874-Escherichia coli,
pubmed-meshheading:12718874-Escherichia coli Proteins,
pubmed-meshheading:12718874-Gene Expression Regulation, Bacterial,
pubmed-meshheading:12718874-Macromolecular Substances,
pubmed-meshheading:12718874-Molecular Conformation,
pubmed-meshheading:12718874-Molecular Sequence Data,
pubmed-meshheading:12718874-Molecular Structure,
pubmed-meshheading:12718874-Plasmids,
pubmed-meshheading:12718874-Prokaryotic Cells,
pubmed-meshheading:12718874-Protein Structure, Tertiary,
pubmed-meshheading:12718874-Sequence Homology, Amino Acid
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pubmed:year |
2003
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pubmed:articleTitle |
Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition.
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pubmed:affiliation |
Laboratories of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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