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Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATP...

Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATP...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_0d4eadeac2dd4b0fac9c841dfb4fef71

Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATPases

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Copper transporting P-type (P
1B-1
-) ATPases are essential for cellular homeostasis. Nonetheless, the E1-E1P-E2P-E2 states mechanism of P
1B-1
-ATPases remains poorly understood. In particular, the role of the intrinsic metal binding domains (MBDs) is enigmatic. Here, four cryo-EM structures and molecular dynamics simulations of a P

Alternative Titles

Full title

Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATPases

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_0d4eadeac2dd4b0fac9c841dfb4fef71

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_0d4eadeac2dd4b0fac9c841dfb4fef71

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-024-47001-4

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