Structure and ion-release mechanism of P<sub>IB-4</sub>-type ATPases.
Ontology highlight
ABSTRACT: Transition metals, such as zinc, are essential micronutrients in all organisms, but also highly toxic in excessive amounts. Heavy-metal transporting P-type (PIB) ATPases are crucial for homeostasis, conferring cellular detoxification and redistribution through transport of these ions across cellular membranes. No structural information is available for the PIB-4-ATPases, the subclass with the broadest cargo scope, and hence even their topology remains elusive. Here, we present structures and complementary functional analyses of an archetypal PIB-4-ATPase, sCoaT from Sulfitobacter sp. NAS14-1. The data disclose the architecture, devoid of classical so-called heavy-metal-binding domains (HMBDs), and provide fundamentally new insights into the mechanism
SUBMITTER: Gronberg C
PROVIDER: S-EPMC8880997 | biostudies-literature | 2021 Dec
REPOSITORIES: biostudies-literature
ACCESS DATA