Seminar: Tracking P-type ATPase native structural dynamics in real time

P-type ATPase transport is carried out in a complex lipid environment and is regulated by both external and internal factors. We have developed a methodology to track P-type ATPase domain rearrangements in real time triggered by laser-induced release of ATP and subsequent monitoring by synchrotron X-ray pulses. This time-resolved X-ray solution scattering (TR-XSS) technique was used to capture the dynamics of an equilibrium state of the sarco/endoplasmic reticulum Ca2+ ATPase (SERCA1a), and transient states at 1.5 and 13 milliseconds. The 13-millisecond state showed a previously unresolved actuator (A) domain arrangement that exposed the ADP-binding site after phosphorylation. We have now identified subtle differences in SERCA1a dynamics that depend on Ca2+ concentration. In addition, we have characterized internal regulation in the isoform SERCA2b and lipid dependence in a bacterial Ca2+ ATPase (LMCA1). The TR-XSS technique presents a unique possibility to simultaneously determine kinetics and structural rearrangements in P-type ATPases to better understand the transport reactions and their regulation.      

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