Structural basis of ion uptake in copper-transporting P1B-type ATPases

Nina Salustros, Christina Grønberg, Nisansala S. Abeyrathna, Pin Lyu, Fredrik Orädd, Kaituo Wang, Magnus Andersson, Gabriele Meloni and Pontus Gourdon ()
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Nina Salustros: Copenhagen University
Christina Grønberg: Copenhagen University
Nisansala S. Abeyrathna: The University of Texas at Dallas
Pin Lyu: Copenhagen University
Fredrik Orädd: Umeå University
Kaituo Wang: Copenhagen University
Magnus Andersson: Umeå University
Gabriele Meloni: The University of Texas at Dallas
Pontus Gourdon: Copenhagen University

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract Copper is essential for living cells, yet toxic at elevated concentrations. Class 1B P-type (P1B-) 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 P1B-ATPases, hampering mechanistic understanding. Here, we present structures that reach 2.7 Å resolution of a copper-specific P1B-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 P1B-mediated transport, likely applicable also to human P1B-members.

Date: 2022
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DOI: 10.1038/s41467-022-32751-w

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