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Efflux pump systems have evolved in bacteria to act as a chemotherapeutic drug and antibiotic resistance mechanism within the bacterial cytoplasmic membrane. These pump systems typically consist of multiple proteins that are embedded in the membranes and perisplasms of the bacterial cells, which all bond together to work to recognize and export foreign materials that have come in contact with the cell. They also play an essential role in biofilm formation of capable bacteria, and work to help provide protection and reduce the stress placed on the biofilm core. | Efflux pump systems have evolved in bacteria to act as a chemotherapeutic drug and antibiotic resistance mechanism within the bacterial cytoplasmic membrane. These pump systems typically consist of multiple proteins that are embedded in the membranes and perisplasms of the bacterial cells, which all bond together to work to recognize and export foreign materials that have come in contact with the cell. They also play an essential role in biofilm formation of capable bacteria, and work to help provide protection and reduce the stress placed on the biofilm core. | ||
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1IWG is one component of a three-part AcrAB-TolC multidrug efflux pump system found in E. coli that works to maintain resistance against a range of antibiotics. This protein, which is also called the bacterial multidrug efflux transporter AcrB protein, works together with the AcrA and TolC proteins to capture and export any antibacterial compounds and detergents that can compromise the cell. 1IWG is the inner-membrane transporter protein in this system and has subunits that are present in both the cytoplasm and periplasm of the E. coli cell, which allows it to work in tandem with the TolC protein for drug export. It is believed that AcrB captures substrates mainly from the periplasm of the cell, but these substrates can still enter the inner cavity of this funnel-like protein from the cytoplasm. | 1IWG is one component of a three-part AcrAB-TolC multidrug efflux pump system found in E. coli that works to maintain resistance against a range of antibiotics. This protein, which is also called the bacterial multidrug efflux transporter AcrB protein, works together with the AcrA and TolC proteins to capture and export any antibacterial compounds and detergents that can compromise the cell. 1IWG is the inner-membrane transporter protein in this system and has subunits that are present in both the cytoplasm and periplasm of the E. coli cell, which allows it to work in tandem with the TolC protein for drug export. It is believed that AcrB captures substrates mainly from the periplasm of the cell, but these substrates can still enter the inner cavity of this funnel-like protein from the cytoplasm. | ||
Revision as of 18:43, 28 April 2022
Bacterial Multidrug Efflux Transporter AcrB (1IWG)
Efflux pump systems have evolved in bacteria to act as a chemotherapeutic drug and antibiotic resistance mechanism within the bacterial cytoplasmic membrane. These pump systems typically consist of multiple proteins that are embedded in the membranes and perisplasms of the bacterial cells, which all bond together to work to recognize and export foreign materials that have come in contact with the cell. They also play an essential role in biofilm formation of capable bacteria, and work to help provide protection and reduce the stress placed on the biofilm core.
1IWG is one component of a three-part AcrAB-TolC multidrug efflux pump system found in E. coli that works to maintain resistance against a range of antibiotics. This protein, which is also called the bacterial multidrug efflux transporter AcrB protein, works together with the AcrA and TolC proteins to capture and export any antibacterial compounds and detergents that can compromise the cell. 1IWG is the inner-membrane transporter protein in this system and has subunits that are present in both the cytoplasm and periplasm of the E. coli cell, which allows it to work in tandem with the TolC protein for drug export. It is believed that AcrB captures substrates mainly from the periplasm of the cell, but these substrates can still enter the inner cavity of this funnel-like protein from the cytoplasm.
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