Atomistic molecular dynamics simulations revealed that intermediate structures in the E1P-E2P transition of Ca2+-ATPase are stabilized by transient sidechain interactions and lipid molecules.
Atomistic molecular dynamics simulations reveal that intermediate structures in the E1P-E2P transition of Ca2+-ATPase are stabilized by transient domain and lipid interactions.
Significance Ion pumps (or P-type ATPases) are membrane proteins, which transport ions through biological membranes against a concentration gradient, a function essential for many biological processes, such as muscle contraction, neurotransmission, and metabolism. Molecular mechanisms underlying active ion transport by ion pumps have been investigated by biochemical experiments and high-resolution structure analyses. Here, the transition of sarcoplasmic reticulum Ca 2+ -ATPase upon dissociation of Ca 2+ is investigated using atomistic molecular dynamics simulations. We find intermediate structures along the pathway are stabilized by transient interactions between A- and P-domains as well as lipid molecules in the transmembrane helices.
Kobayashi et al. (Thu,) conducted a other in Sarcoplasmic reticulum Ca2+-ATPase function. Atomistic molecular dynamics simulations was evaluated on Structural and energetic changes during the E1P-E2P transition. Atomistic molecular dynamics simulations revealed that intermediate structures in the E1P-E2P transition of Ca2+-ATPase are stabilized by transient sidechain interactions and lipid molecules.
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