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Copper-transporting P-type ATPases use a unique ion-release pathway

Copper-transporting P-type ATPases use a unique ion-release pathway

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3904665

Copper-transporting P-type ATPases use a unique ion-release pathway

About this item

Full title

Copper-transporting P-type ATPases use a unique ion-release pathway

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2014-01, Vol.21 (1), p.43-48

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

P-type ATPases adopt different conformations during their transport cycle, including autophosphorylated forms. The structure of type IB P-type ATPase CopA is now solved in its E2P state. Comparison with a previous E2Pi structure indicates that dephosphorylation is not coupled to ion extrusion, in contrast to mechanisms in type IIA SERCA. The findin...

Alternative Titles

Full title

Copper-transporting P-type ATPases use a unique ion-release pathway

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3904665

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3904665

Other Identifiers

ISSN

1545-9993

E-ISSN

1545-9985

DOI

10.1038/nsmb.2721

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