Dynamics of activation in the voltage-sensing domain of Ciona intestinalis phosphatase Ci-VSP.

ABSTRACT: The Ciona intestinalis voltage-sensing phosphatase (Ci-VSP) is a membrane protein containing a voltage-sensing domain (VSD) that is homologous to VSDs from voltage-gated ion channels responsible for cellular excitability. Previously published crystal structures of Ci-VSD in putative resting and active conformations suggested a helical-screw voltage sensing mechanism in which the S4 helix translocates and rotates to enable exchange of salt-bridge partners, but the microscopic details of the transition between the resting and active conformations remained unknown. Here, by combining extensive molecular dynamics simulations with a recently developed computational framework based on dynamical operators, we elucidate the microscopic mechanism of the resting-active transition at physiological me

SUBMITTER: Guo SC 

PROVIDER: S-EPMC10869754 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature