SANS of heavy-metal transporting P-type ATPases
Heavy-metal transporting P-type ATPases move toxic heavy metal ions out of cells. A critical question is how this transport is regulated. Cytoplasmic metal-binding domains (MBD¿s) have been attributed a central role in regulation, but structural information remain scarce. We propose to use SANS to describe the position and conformational freedom of regulating MBD¿s for two heavy-metal transporting P-type ATPases ¿ with specificity for cadmium (CadA) and zinc (ZntA), respectively. We will utilize mutant proteins lacking the MBD¿s, match-out deuterated detergent to avoid scattering contributions from the micelles and ligands to promote specific conformational states. We will use SEC-SANS to collect data with protein aggregation minimized, and for additional liganded conditions we will perform measurements in standard cuvette-mode. To achieve the structural refinement, we will use ensemble optimization combined with molecular dynamics simulations. All in all, these experiments will provide direct structural information on the regulation of heavy metal transport by P-type ATPases.
The data is currently only available to download if you are a member of the proposal team.
The recommended format for citing this dataset in a research publication is in the following format:
LYCKSELL Marie; ANDERSSON Magnus; CATTY Patrice; MAGKAKIS Konstantinos and MARTEL Anne. (2023). SANS of heavy-metal transporting P-type ATPases. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-1076
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