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- W1972648209 abstract "ABC (ATP Binding Cassette) proteins are a large family of membrane transporters dependent on ATP hydrolysis. Members of this family are of interest due to their role in multidrug resistance by bacteria, chemotherapy resistance by tumors, cystic fibrosis, and adrenoleukodystrophy. Transporters consist of a nucleotide binding domain (NBD) and a transmembrane domain (TMD), and in the case of importers, a periplasmic binding protein that binds the substrate and delivers it to the periplasmic side of the transporter. In bacteria, transporters are often symmetric, existing as a homodimer containing two copies of the same polypeptide chain. While the substrates of ABC transporters are many and varied, the NBDs at which ATP hydrolysis occurs are highly conserved across all species. The structure of several members of the ABC family have been solved by X-ray crystallography, however the mechanism by which ATP hydrolysis is linked to the domain rearrangement that facilitates transport is unclear. Molecular dynamics simulations allow the dynamics of a representative ABC importer, the vitamin B12 uptake system (BTU) from E. coli, to be modeled at atomistic detail. The protein is composed of two copies each of BtuC, the TMD, and BtuD, the NBD, as well as the periplasmic binding protein, BtuF. Simulations of the protein in the presence and absence of ATP have been performed in order to observe the effects of ATP binding and hydrolysis on the arrangement of the protein. Simulations of the complete transporter, BtuC2D2F, demonstrate the influence of the binding protein on the structure of the complex." @default.
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- W1972648209 date "2010-01-01" @default.
- W1972648209 modified "2023-09-27" @default.
- W1972648209 title "Molecular Dynamics Simulations of a Bacterial ABC Transporter" @default.
- W1972648209 doi "https://doi.org/10.1016/j.bpj.2009.12.3535" @default.
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