Literature summary for 7.2.2.9 extracted from

Deigweiher, K.; Drell, T.L.; Prutsch, A.; Scheidig, A.J.; Luebben, M.
Expression, isolation, and crystallization of the catalytic domain of CopB, a putative copper transporting ATPase from the thermoacidophilic archaeon Sulfolobus solfataricus (2004), J. Bioenerg. Biomembr., 36, 151-159.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of three different soluble domains of the protein (CopB-A (phosphatase domain), CopB-B, and CopB-C) in Escherichia coli	Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment)	Organism
hangimg drop vapour diffusion method, 3D crystals of CopB-B, the 29 kDa catalytic ATP binding/phosphorylation domain are produced, which diffracted to a resolution of 2.2 A	Saccharolobus solfataricus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	integral membrane protein	Saccharolobus solfataricus	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ag+	stimulates	Saccharolobus solfataricus
Cu2+	CopB-B has heavy metal stimulated phosphatase activity, which is half maximal in the presence of 80 microM Cu2+	Saccharolobus solfataricus
additional information	no stimulation by Cu+	Saccharolobus solfataricus
Zn2+	stimulates	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	Q97UU7	-	-

Purification (Commentary)

Purification (Comment)	Organism
purification of three different soluble domains of the protein (CopB-A), CopB-B (ATP binding/phosphorylation domain), and CopB-C (cation binding domain)	Saccharolobus solfataricus

Synonyms

Synonyms	Comment	Organism
CopB	-	Saccharolobus solfataricus
copper transporting ATPase	-	Saccharolobus solfataricus

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Release 2023.1 (January 2023)