7QC0
Crystal structure of Cadmium translocating P-type ATPase
Summary for 7QC0
| Entry DOI | 10.2210/pdb7qc0/pdb |
| Related | 7QBZ |
| Descriptor | Cadmium translocating P-type ATPase, BERYLLIUM TRIFLUORIDE ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | p-type atpase pib-atpase transporter exporter, membrane protein |
| Biological source | Sulfitobacter sp. (strain NAS-14.1) |
| Total number of polymer chains | 1 |
| Total formula weight | 71744.55 |
| Authors | Groenberg, C.,Hu, Q.,Wang, K.,Gourdon, P. (deposition date: 2021-11-21, release date: 2022-03-23, Last modification date: 2024-01-31) |
| Primary citation | Gronberg, C.,Hu, Q.,Mahato, D.R.,Longhin, E.,Salustros, N.,Duelli, A.,Lyu, P.,Bagenholm, V.,Eriksson, J.,Rao, K.U.,Henderson, D.I.,Meloni, G.,Andersson, M.,Croll, T.,Godaly, G.,Wang, K.,Gourdon, P. Structure and ion-release mechanism of P IB-4 -type ATPases. Elife, 10:-, 2021 Cited by PubMed Abstract: Transition metals, such as zinc, are essential micronutrients in all organisms, but also highly toxic in excessive amounts. Heavy-metal transporting P-type (P) 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 P-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 P-ATPase, sCoaT from 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 and diversity of heavy-metal transporters. We reveal several novel P-type ATPase features, including a dual role in heavy-metal release and as an internal counter ion of an invariant histidine. We also establish that the turnover of P-ATPases is potassium independent, contrasting to many other P-type ATPases. Combined with new inhibitory compounds, our results open up for efforts in for example drug discovery, since P-ATPases function as virulence factors in many pathogens. PubMed: 34951590DOI: 10.7554/eLife.73124 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.11 Å) |
Structure validation
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