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- W2056331341 abstract "Transition metals, such as copper and zinc, are required by a range of different processes in life. However, because excessive levels of these micro-nutrients are also damaging to the cell, careful distribution between cellular compartments and extrusion from the cell are crucial for viability. P-type ATPases of subfamily IB (PIB-ATPases) are key regulators of copper and zinc through active transport of these and other heavy-metals, across membranes. Dysfunction of the human copper-transporting PIB-ATPases, ATP7A and ATP7B, is associated with Menkes and Wilson's disease, respectively, which might be circumvented by stabilizing compounds. On the other hand, the critical role of PIB-ATPases for heavy-metal homeostasis and detoxification in bacteria, fungi, parasites and cancer make them favorable targets for new drugs. Evidently, understanding how copper and zinc-transporting PIB-ATPases, such as the bacterial CopA and ZntA, work at the atomic level will also explain how their function is affected by disease mutations or targeted by inhibitors. Within the PIB-type ATPase subfamily, CopA is the only protein that has had its crystal structure determined (Gourdon et al. 2011) as derived from a crystal structure of the protein stabilized in lipid-detergent micelles. This structure shares the common P-Type ATPase architecture, with an additional large amphipathic helix at the cytoplasmic interface. However, knowledge of the dynamic interplay of the PIB-ATPases with intact lipid bilayers is absent in this structure. Thus, the aims of the current study is to elucidate how CopA and ZntA behave in, and depend on, the surrounding lipid bilayer by utilizing a serial multiscale molecular dynamics approach by combining coarse-grained and atomistic simulations. This approach affords insight into an otherwise evasive system." @default.
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- W2056331341 date "2014-01-01" @default.
- W2056331341 modified "2023-09-30" @default.
- W2056331341 title "Dynamics of Transition Metal Transporting P-Type ATPases in Native Membranes" @default.
- W2056331341 doi "https://doi.org/10.1016/j.bpj.2013.11.622" @default.
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