Redistribution of SERCA calcium pump conformers during intracellular calcium signaling.

ABSTRACT: The conformational changes of a calcium transport ATPase were investigated with molecular dynamics (MD) simulations as well as fluorescence resonance energy transfer (FRET) measurements to determine the significance of a discrete structural element for regulation of the conformational dynamics of the transport cycle. Previous MD simulations indicated that a loop in the cytosolic domain of the SERCA calcium transporter facilitates an open-to-closed structural transition. To investigate the significance of this structural element, we performed additional MD simulations and new biophysical measurements of SERCA structure and function. Rationally designed in silico mutations of three acidic residues of the loop decreased SERCA domain-domain contacts and increased domain-domain separatio

SUBMITTER: Raguimova ON 

PROVIDER: S-EPMC6052202 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature