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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2008-11-5
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pubmed:databankReference |
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pubmed:abstractText |
Bacterial pathogens have evolved a sophisticated arsenal of virulence factors to modulate host cell biology. Enteropathogenic and enterohemorrhagic Escherichia coli (EPEC and EHEC) use a type III protein secretion system (T3SS) to inject microbial proteins into host cells. The T3SS effector cycle inhibiting factor (Cif) produced by EPEC and EHEC is able to block host eukaryotic cell-cycle progression. We present here a crystal structure of Cif, revealing it to be a divergent member of the superfamily of enzymes including cysteine proteases and acetyltransferases that share a common catalytic triad. Mutation of these conserved active site residues abolishes the ability of Cif to block cell-cycle progression. Finally, we demonstrate that irreversible cysteine protease inhibitors do not abolish the Cif cytopathic effect, suggesting that another enzymatic activity may underlie the biological activity of this virulence factor.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-10089316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-10597228,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-10876241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-11030657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-11090361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-11104681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-11368758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-11598051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-12062101,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-14651638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-14681400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-14694194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-14696379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-15164065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-15292151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-15299911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-15694849,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-15694861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-15737728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-15746386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-15845459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-16728640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-16848790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-16902142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-17136086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-6502713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-7845226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-8578593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-8702770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18845161-9621195
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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 |
Dec
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pubmed:issn |
1089-8638
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
12
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pubmed:volume |
384
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
465-77
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:18845161-Actins,
pubmed-meshheading:18845161-Amino Acid Sequence,
pubmed-meshheading:18845161-Caseins,
pubmed-meshheading:18845161-Catalysis,
pubmed-meshheading:18845161-Cell Cycle,
pubmed-meshheading:18845161-Chromatography, Gel,
pubmed-meshheading:18845161-Crystallography, X-Ray,
pubmed-meshheading:18845161-Cysteine Endopeptidases,
pubmed-meshheading:18845161-Enzyme Activation,
pubmed-meshheading:18845161-Escherichia coli,
pubmed-meshheading:18845161-Escherichia coli Proteins,
pubmed-meshheading:18845161-HeLa Cells,
pubmed-meshheading:18845161-Humans,
pubmed-meshheading:18845161-Models, Molecular,
pubmed-meshheading:18845161-Molecular Sequence Data,
pubmed-meshheading:18845161-Phenotype,
pubmed-meshheading:18845161-Protease Inhibitors,
pubmed-meshheading:18845161-Protein Structure, Secondary,
pubmed-meshheading:18845161-Sequence Deletion,
pubmed-meshheading:18845161-Stress Fibers,
pubmed-meshheading:18845161-Structural Homology, Protein,
pubmed-meshheading:18845161-Substrate Specificity
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pubmed:year |
2008
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pubmed:articleTitle |
Structure of the cyclomodulin Cif from pathogenic Escherichia coli.
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pubmed:affiliation |
Laboratory of Structural Microbiology, Rockefeller University, New York, NY 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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