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...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2004
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| _version_ | 1797091303181254656 |
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| author | Fernandez-Recio, J Walas, F Federici, L Venkatesh Pratap, J Bavro, V Miguel, R Mizuguchi, K Luisi, B |
| author_facet | Fernandez-Recio, J Walas, F Federici, L Venkatesh Pratap, J Bavro, V Miguel, R Mizuguchi, K Luisi, B |
| author_sort | Fernandez-Recio, J |
| collection | OXFORD |
| 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. |
| first_indexed | 2024-03-07T03:31:03Z |
| format | Journal article |
| id | oxford-uuid:baba2386-04f4-4a17-9182-5c344364d60b |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:31:03Z |
| publishDate | 2004 |
| record_format | dspace |
| spelling | oxford-uuid:baba2386-04f4-4a17-9182-5c344364d60b2022-03-27T05:11:46ZA model of a transmembrane drug-efflux pump from Gram-negative bacteria.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:baba2386-04f4-4a17-9182-5c344364d60bEnglishSymplectic Elements at Oxford2004Fernandez-Recio, JWalas, FFederici, LVenkatesh Pratap, JBavro, VMiguel, RMizuguchi, KLuisi, BIn 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. |
| spellingShingle | Fernandez-Recio, J Walas, F Federici, L Venkatesh Pratap, J Bavro, V Miguel, R Mizuguchi, K Luisi, B A model of a transmembrane drug-efflux pump from Gram-negative bacteria. |
| title | A model of a transmembrane drug-efflux pump from Gram-negative bacteria. |
| title_full | A model of a transmembrane drug-efflux pump from Gram-negative bacteria. |
| title_fullStr | A model of a transmembrane drug-efflux pump from Gram-negative bacteria. |
| title_full_unstemmed | A model of a transmembrane drug-efflux pump from Gram-negative bacteria. |
| title_short | A model of a transmembrane drug-efflux pump from Gram-negative bacteria. |
| title_sort | model of a transmembrane drug efflux pump from gram negative bacteria |
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