Copper-transporting P-type ATPases use a unique ion-release pathway
Copper-transporting P-type ATPases use a unique ion-release pathway
About this item
Full title
Author / Creator
Publisher
New York: Nature Publishing Group US
Journal title
Language
English
Formats
Publication information
Publisher
New York: Nature Publishing Group US
Subjects
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
Authors, Artists and Contributors
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