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

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

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_c8cb1d926b1a4d6ba114c37bb55f2a73

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

About this item

Full title

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

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2022-08, Vol.13 (1), p.1-11, Article 5121

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Copper is essential for living cells, yet toxic at elevated concentrations. Class 1B P-type (P
1B
-) 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...

Alternative Titles

Full title

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

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_c8cb1d926b1a4d6ba114c37bb55f2a73

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_c8cb1d926b1a4d6ba114c37bb55f2a73

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-022-32751-w

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