Literature summary for 7.2.2.8 extracted from

Gronberg, C.; Sitsel, O.; Lindahl, E.; Gourdon, P.; Andersson, M.
Membrane anchoring and ion-entry dynamics in P-type ATPase copper transport (2016), Biophys. J., 111, 2417-2429 .

Search for more literature for 7.2.2.8

Crystallization (Commentary)

Crystallization (Comment)	Organism
structural modeling. The ion-entry path involves one transient Met148-Cys382 ion-binding site and one intramembranous site formed by trigonal coordination to Cys384, Asn689, and Met717. The protein anchors predominantly in the cytoplasmic leaflet with exposed positive charges on the putative MB docking platform	Legionella pneumophila subsp. pneumophila

Protein Variants

Protein Variants	Comment	Organism
D426N	inactive	Legionella pneumophila subsp. pneumophila
K135E/R136E	almost complete loss of activity	Legionella pneumophila subsp. pneumophila
K135S	significant reduction of activity	Legionella pneumophila subsp. pneumophila
K135S/K142S	almost complete loss of activity	Legionella pneumophila subsp. pneumophila
K142S	significant reduction of activity	Legionella pneumophila subsp. pneumophila
R136S	significant reduction of activity	Legionella pneumophila subsp. pneumophila

Organism

Organism	UniProt	Comment	Textmining
Legionella pneumophila subsp. pneumophila	Q5ZWR1	-	-
Legionella pneumophila subsp. pneumophila DSM 7513	Q5ZWR1	-	-

Synonyms

Synonyms	Comment	Organism
copper-exporting P-type ATPase	-	Legionella pneumophila subsp. pneumophila

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Release 2023.1 (January 2023)