Sandbox Reserved 689
From Proteopedia
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<scene name='Sandbox_Reserved_689/Rifampicin_in_acrb_l_monomer/1'>Rifampicin bound in proximal binding pocket</scene> | <scene name='Sandbox_Reserved_689/Rifampicin_in_acrb_l_monomer/1'>Rifampicin bound in proximal binding pocket</scene> | ||
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+ | == Substrates == | ||
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+ | Because of the large binding pockets in AcrB, it is able to bind and export a wide variety of antibiotic drugs and other toxins. | ||
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+ | '''Rifampicin:''' | ||
+ | <scene name='Sandbox_Reserved_689/Rifampicin_in_acrb/1'>Bound; entire AcrB trimer shown</scene> | ||
+ | <scene name='Sandbox_Reserved_689/Rifampicin_in_acrb_monomer/1'>Binding Pocket Close Up</scene>, interacting residues (all residues within 4 Angstroms) highlighted and shown in ball-and-stick representation. | ||
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+ | <scene name='Sandbox_Reserved_689/Rifampicin_in_acrb_polar_non/2'>TextToBeDisplayed</scene> | ||
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Revision as of 14:01, 30 April 2013
This Sandbox is Reserved from 30/01/2013, through 30/12/2013 for use in the course "Biochemistry II" taught by Hannah Tims at the Messiah College. This reservation includes Sandbox Reserved 686 through Sandbox Reserved 700. |
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The E. coli AcrB Efflux Pump
Structure
The AcrB efflux pump is part of a tripartite system used by E. Coli to remove antibiotic and other toxic molecules from the bacterial cell.
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Substrates
Because of the large binding pockets in AcrB, it is able to bind and export a wide variety of antibiotic drugs and other toxins.
Rifampicin: , interacting residues (all residues within 4 Angstroms) highlighted and shown in ball-and-stick representation.
Energy Transduction
There are (Asp408, Asp407, Lys940, and Arg 971) whose protonation and deprotonation are suggested to play a large role in the conformational change between the L, T, and O states (Eicher, et al. 2009). PDB: 3D9B