A model of a transmembrane drug-efflux pump from Gram-negative bacteria
In Gram-negative bacteria, drug resistance is due in part to the activity of transmembrane efflux-pumps, which are composed of three types of proteins. A representative pump from Escherichia coli is an assembly of the trimeric outer-membrane protein TolC, which is an allosteric channel, the trimeric...
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| Veröffentlicht in: | FEBS letters 2004-12, Vol.578 (1), p.5-9 |
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| creator | Fernandez-Recio, Juan Walas, Fabien Federici, Luca Venkatesh Pratap, J. Bavro, Vassiliy N. Miguel, Ricardo Nunez Mizuguchi, Kenji Luisi, Ben |
| description | In Gram-negative bacteria, drug resistance is due in part to the activity of transmembrane efflux-pumps, which are composed of three types of proteins. A representative pump from
Escherichia coli is an assembly of the trimeric outer-membrane protein TolC, which is an allosteric channel, the trimeric inner-membrane proton-antiporter AcrB, and the periplasmic protein, AcrA. The pump displaces drugs vectorially from the bacterium using proton electrochemical force. Crystal structures are available for TolC and AcrB from
E. coli, and for the AcrA homologue MexA from
Pseudomonas aeruginosa. Based on homology modelling and molecular docking, we show how AcrA, AcrB and TolC might assemble to form a tripartite pump, and how allostery may occur during transport. |
| doi_str_mv | 10.1016/j.febslet.2004.10.097 |
| format | Article |
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Escherichia coli is an assembly of the trimeric outer-membrane protein TolC, which is an allosteric channel, the trimeric inner-membrane proton-antiporter AcrB, and the periplasmic protein, AcrA. The pump displaces drugs vectorially from the bacterium using proton electrochemical force. Crystal structures are available for TolC and AcrB from
E. coli, and for the AcrA homologue MexA from
Pseudomonas aeruginosa. Based on homology modelling and molecular docking, we show how AcrA, AcrB and TolC might assemble to form a tripartite pump, and how allostery may occur during transport.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2004.10.097</identifier><identifier>PMID: 15581607</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Bacterial Outer Membrane Proteins - chemistry ; Bacterial Outer Membrane Proteins - metabolism ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; Drug Resistance, Microbial ; Escherichia coli ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Gram-Negative Bacteria - physiology ; Homology modelling ; inner-membrane ; major facilitator superfamily ; membrane fusion protein ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Membrane Transport Proteins - chemistry ; Membrane Transport Proteins - metabolism ; MFP ; MFS ; Models, Biological ; Models, Molecular ; Molecular docking and allostery ; Multidrug resistance ; Multidrug Resistance-Associated Proteins ; outer-membrane ; Protein Conformation ; Pseudomonas aeruginosa ; Pump-channel ; resistance-nodulation-division ; RND ; Transmembrane transport</subject><ispartof>FEBS letters, 2004-12, Vol.578 (1), p.5-9</ispartof><rights>2004</rights><rights>FEBS Letters 578 (2004) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4577-9937f6c89fb6270e65b8f090467d44610c964ac2348273d492c8420b77e2a0d43</citedby><cites>FETCH-LOGICAL-c4577-9937f6c89fb6270e65b8f090467d44610c964ac2348273d492c8420b77e2a0d43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2004.10.097$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579304013687$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15581607$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fernandez-Recio, Juan</creatorcontrib><creatorcontrib>Walas, Fabien</creatorcontrib><creatorcontrib>Federici, Luca</creatorcontrib><creatorcontrib>Venkatesh Pratap, J.</creatorcontrib><creatorcontrib>Bavro, Vassiliy N.</creatorcontrib><creatorcontrib>Miguel, Ricardo Nunez</creatorcontrib><creatorcontrib>Mizuguchi, Kenji</creatorcontrib><creatorcontrib>Luisi, Ben</creatorcontrib><title>A model of a transmembrane drug-efflux pump from Gram-negative bacteria</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>In Gram-negative bacteria, drug resistance is due in part to the activity of transmembrane efflux-pumps, which are composed of three types of proteins. A representative pump from
Escherichia coli is an assembly of the trimeric outer-membrane protein TolC, which is an allosteric channel, the trimeric inner-membrane proton-antiporter AcrB, and the periplasmic protein, AcrA. The pump displaces drugs vectorially from the bacterium using proton electrochemical force. Crystal structures are available for TolC and AcrB from
E. coli, and for the AcrA homologue MexA from
Pseudomonas aeruginosa. Based on homology modelling and molecular docking, we show how AcrA, AcrB and TolC might assemble to form a tripartite pump, and how allostery may occur during transport.</description><subject>Bacterial Outer Membrane Proteins - chemistry</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>Drug Resistance, Microbial</subject><subject>Escherichia coli</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Gram-Negative Bacteria - physiology</subject><subject>Homology modelling</subject><subject>inner-membrane</subject><subject>major facilitator superfamily</subject><subject>membrane fusion protein</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Transport Proteins - chemistry</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>MFP</subject><subject>MFS</subject><subject>Models, Biological</subject><subject>Models, Molecular</subject><subject>Molecular docking and allostery</subject><subject>Multidrug resistance</subject><subject>Multidrug Resistance-Associated Proteins</subject><subject>outer-membrane</subject><subject>Protein Conformation</subject><subject>Pseudomonas aeruginosa</subject><subject>Pump-channel</subject><subject>resistance-nodulation-division</subject><subject>RND</subject><subject>Transmembrane transport</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1r3DAQhkVpabZpf0KLTrl5M5JlfZxKEpJNIJBD27OQ5VHQYq23kp2Pf1-bXcgxPQ0a3nk0PEPIdwZrBkyeb9cB29LjuOYAYu6twagPZMW0qqtaSP2RrACYqBpl6hPypZQtzG_NzGdywppGMwlqRTYXNA0d9nQI1NExu11JmNq5Iu3y9FhhCP30QvdT2tOQh0Q32aVqh49ujE9IW-dHzNF9JZ-C6wt-O9ZT8ufm-vfVbXX_sLm7urivvGiUqoypVZBem9BKrgBl0-oABoRUnRCSgTdSOM9robmqO2G414JDqxRyB52oT8nZgbvPw98Jy2hTLB77fl54mIqVijWcSf1ukBkFhsuF2ByCPg-lZAx2n2Ny-dUysItqu7VH1XZRvbRn1fPcj-MHU5uwe5s6up0Dt4fAc-zx9f-o9ub6kv9a7racDQSwWuoF9fOAwlntU8Rsi4-489jFjH603RDf2fYf1n-lkw</recordid><startdate>20041203</startdate><enddate>20041203</enddate><creator>Fernandez-Recio, Juan</creator><creator>Walas, Fabien</creator><creator>Federici, Luca</creator><creator>Venkatesh Pratap, J.</creator><creator>Bavro, Vassiliy N.</creator><creator>Miguel, Ricardo Nunez</creator><creator>Mizuguchi, Kenji</creator><creator>Luisi, Ben</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20041203</creationdate><title>A model of a transmembrane drug-efflux pump from Gram-negative bacteria</title><author>Fernandez-Recio, Juan ; 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Escherichia coli is an assembly of the trimeric outer-membrane protein TolC, which is an allosteric channel, the trimeric inner-membrane proton-antiporter AcrB, and the periplasmic protein, AcrA. The pump displaces drugs vectorially from the bacterium using proton electrochemical force. Crystal structures are available for TolC and AcrB from
E. coli, and for the AcrA homologue MexA from
Pseudomonas aeruginosa. Based on homology modelling and molecular docking, we show how AcrA, AcrB and TolC might assemble to form a tripartite pump, and how allostery may occur during transport.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>15581607</pmid><doi>10.1016/j.febslet.2004.10.097</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Online Library Free Content; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - metabolism Carrier Proteins - chemistry Carrier Proteins - metabolism Drug Resistance, Microbial Escherichia coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Gram-Negative Bacteria - physiology Homology modelling inner-membrane major facilitator superfamily membrane fusion protein Membrane Proteins - chemistry Membrane Proteins - metabolism Membrane Transport Proteins - chemistry Membrane Transport Proteins - metabolism MFP MFS Models, Biological Models, Molecular Molecular docking and allostery Multidrug resistance Multidrug Resistance-Associated Proteins outer-membrane Protein Conformation Pseudomonas aeruginosa Pump-channel resistance-nodulation-division RND Transmembrane transport |
| title | A model of a transmembrane drug-efflux pump from Gram-negative bacteria |
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