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- W1977091076 abstract "ATP Binding Cassette (ABC) transporters are transmembrane transporters that use the energy released by ATP hydrolysis to transport a wide array of substrates. They are found in all kingdoms of life, and are complicit in various genetic conditions, such as cystic fibrosis, macular degeneration, and multi-drug resistance. The E. coli ribose transporter (RbsABC) is a multisubunit ABC transporter complex with a periplasmic ribose binding domain, a transmembrane domain dimer, and a cytoplasmic nucleotide binding domain. The ribose transport complex has been shown to assemble and disassemble into distinct combinations of the subunits based on the presence of cofactors (ATP and analogues, ADP, orthovanadate, and magnesium), suggesting a series of steps for how the subunits associate and subsequently transport ribose. To further explore the conformation of the subunits in response to these different sets of cofactors, cysteine mutations were introduced to allow the addition of EPR spin labels. These labeled mutants will be used to determine whether subunits are bound. Additionally, double mutants will be used to elucidate conformational state of subunits." @default.
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- W1977091076 date "2010-01-01" @default.
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- W1977091076 title "Exploring Conformational Changes in the RbsABC Transporter Using EPR Spin Labeling" @default.
- W1977091076 doi "https://doi.org/10.1016/j.bpj.2009.12.312" @default.
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