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- W1992046105 abstract "Cellular copper levels are carefully controlled to avoid toxic free copper while maintaining integrity of enzymatic copper centers. PIB-type ATPases transport Cu+ ions across membranes with high specificity. Here, we use a range of molecular dynamics (MD) simulation techniques in combination with enzymatic assays and x-ray crystallography to determine the copper-transport pathway mediated by a Cu+ transporting P-type ATPase (CopA). The simulation data provide insight into transport energetics and accompanying side-chain interactions that would be hard to observe experimentally. We also observed a unique mode of ion transport, where the dephosphorylation event was not obligatory coupled to the structural rearrangements that produce an occluded intermediate state. Hence, the generalized reaction scheme based on PII-type ATPases, such as SERCA, might not apply to all P-type ATPases.Figure 1: The simulated energetics associated with copper release.View Large Image | View Hi-Res Image | Download PowerPoint Slide" @default.
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- W1992046105 date "2014-01-01" @default.
- W1992046105 modified "2023-10-03" @default.
- W1992046105 title "Transport Pathway in Cu+ P-Type ATPases" @default.
- W1992046105 doi "https://doi.org/10.1016/j.bpj.2013.11.2406" @default.
- W1992046105 hasPublicationYear "2014" @default.
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