7R0G

STRUCTURAL BASIS OF ION UPTAKE IN COPPER-TRANSPORTING P1B-TYPE ATPASES

Summary for 7R0G

• Entry DOI: 10.2210/pdb7r0g/pdb
• Descriptor: Putative copper-exporting P-type ATPase A (1 entity in total)
• Functional Keywords: atpase, membrane protein
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 2
• Total formula weight: 140822.17

Authors

Salustros, N.,Groenberg, C.,Wang, K.,Gourdon, P. (deposition date: 2022-02-02, release date: 2022-09-14, Last modification date: 2024-01-31)

Primary citation

Salustros, N.,Gronberg, C.,Abeyrathna, N.S.,Lyu, P.,Oradd, F.,Wang, K.,Andersson, M.,Meloni, G.,Gourdon, P.
Structural basis of ion uptake in copper-transporting P 1B -type ATPases.
Nat Commun, 13:5121-5121, 2022

PubMed Abstract: Copper is essential for living cells, yet toxic at elevated concentrations. Class 1B P-type (P-) ATPases are present in all kingdoms of life, facilitating cellular export of transition metals including copper. P-type ATPases follow an alternating access mechanism, with inward-facing E1 and outward-facing E2 conformations. Nevertheless, no structural information on E1 states is available for P-ATPases, hampering mechanistic understanding. Here, we present structures that reach 2.7 Å resolution of a copper-specific P-ATPase in an E1 conformation, with complementing data and analyses. Our efforts reveal a domain arrangement that generates space for interaction with ion donating chaperones, and suggest a direct Cu transfer to the transmembrane core. A methionine serves a key role by assisting the release of the chaperone-bound ion and forming a cargo entry site together with the cysteines of the CPC signature motif. Collectively, the findings provide insights into P-mediated transport, likely applicable also to human P-members.

PubMed: 36045128
DOI: 10.1038/s41467-022-32751-w

Experimental method

X-RAY DIFFRACTION (4.01 Å)