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Highlights • A time-resolved synchrotron setup for tracking protein dynamics was developed • Laser-induced activation of caged ATP triggered the adenylate kinase reaction • The achieved time resolution was 2 ms for a monitoring time of 50 ms • Effects of radiation damage were characterized and minimized Summary Protein dynamics are essential to biological function, and methods to determine such structural rearrangements constitute a frontier in structural biology.
Abstract Copper transporting P-type (P1B-1-) ATPases are essential for cellular homeostasis. Nonetheless, the E1-E1P-E2P-E2 states mechanism of P1B-1-ATPases remains poorly understood. In particular, the role of the intrinsic metal binding domains (MBDs) is enigmatic.
The N-terminal tail extension stems from changes in MBD2, MBD3 and MBD5 dynamics Because the locations of MBD2, MBD3, and MBD5 differed significantly between holo and apo simulations, we dissected their positions into x, y, and z center-of-mass coordinates to better resolve inter-domain dynamics, where x and y are in the plane of the membrane and z is perpendicular to the membrane.
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