Structures of a sperm-specific solute carrier gated by voltage and cAMP.

ABSTRACT: The newly characterized sperm-specific Na⁺/H⁺ exchanger stands out by its unique tripartite domain composition^1,2. It unites a classical solute carrier unit with regulatory domains usually found in ion channels, namely, a voltage-sensing domain and a cyclic-nucleotide binding domain^1,3, which makes it a mechanistic chimera and a secondary-active transporter activated strictly by membrane voltage. Our structures of the sea urchin SpSLC9C1 in the absence and presence of ligands reveal the overall domain arrangement and new structural coupling elements. They allow us to propose a gating model, where movements in the voltage sensor indirectly cause the release of the exchanging unit from a locked state through long-distance allosteric effects transmi

SUBMITTER: Kalienkova V 

PROVIDER: S-EPMC10620091 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature