Source:http://linkedlifedata.com/resource/pubmed/id/11589692
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
19
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pubmed:dateCreated |
2001-10-8
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pubmed:abstractText |
Gram-negative bacteria are enveloped by a system of two membranes, and they use specialized multicomponent, energy-driven pumps to transport molecules directly across this double-layered partition from the cell interior to the extra-cellular environment. One component of these pumps is embedded in the outer-membrane, and the paradigm for its structure and function is the TolC protein from Escherichia coli. A common component of a wide variety of efflux pumps, TolC and its homologues are involved in the export of chemically diverse molecules ranging from large protein toxins, such as alpha-hemolysin, to small toxic compounds, such as antibiotics. TolC family members thus play important roles in conferring pathogenic bacteria with both virulence and multidrug resistance. These pumps assemble reversibly in a transient process that brings together TolC or its homologue, an inner-membrane-associated periplasmic component, an integral inner-membrane translocase and the substrate itself. TolC can associate in this fashion with a variety of different partners to participate in the transport of diverse substrates. We review here the structure and function of TolC and the other components of the efflux/transport pump.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Pharmaceutical Preparations,
http://linkedlifedata.com/resource/pubmed/chemical/tolC protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5011-26
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:11589692-Bacterial Outer Membrane Proteins,
pubmed-meshheading:11589692-Biological Transport,
pubmed-meshheading:11589692-Escherichia coli Proteins,
pubmed-meshheading:11589692-Membrane Fusion,
pubmed-meshheading:11589692-Membrane Transport Proteins,
pubmed-meshheading:11589692-Models, Molecular,
pubmed-meshheading:11589692-Pharmaceutical Preparations,
pubmed-meshheading:11589692-Protein Conformation,
pubmed-meshheading:11589692-Protein Transport,
pubmed-meshheading:11589692-Stereoisomerism
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pubmed:year |
2001
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pubmed:articleTitle |
The role of the TolC family in protein transport and multidrug efflux. From stereochemical certainty to mechanistic hypothesis.
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pubmed:affiliation |
Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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