Literature summary for 7.2.2.10 extracted from

Jidenko, M.; Nielsen, R.C.; S?rensen, T.L.; M?ller, J.V.; le Maire, M.; Nissen, P.; Jaxel, C.
Crystallization of a mammalian membrane protein overexpressed in Saccharomyces cerevisiae (2005), Proc. Natl. Acad. Sci. USA, 102, 11687-11691.

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of C-terminally biotinylated SERCA1a, with introduced thrombin cleavage site, in Saccharomyces cerevisiae	Oryctolagus cuniculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, hanging drop vapour diffusion method, 12 mg/ml protein in a solution containing 10 mM Ca2+, 1 mm beta,gamma-methyleneadenosine 5'-triphosphate, and 1,2-dioleoyl-sn-glycero-3-phosphocholine, 0.002 ml is mixed with 0.002 ml well solution containing 0.2 M sodium acetate, 10-14% w/v PEG 6000, 10% glycerol, and 4% tert-butanol, crystals grow within 1 to 14 days at 19°C, X-ray diffraction structure determination and analysis at 3.3 A resolution	Oryctolagus cuniculus

Crystallization (Comment)

Organism

purified recombinant enzyme, hanging drop vapour diffusion method, 12 mg/ml protein in a solution containing 10 mM Ca2+, 1 mm beta,gamma-methyleneadenosine 5'-triphosphate, and 1,2-dioleoyl-sn-glycero-3-phosphocholine, 0.002 ml is mixed with 0.002 ml well solution containing 0.2 M sodium acetate, 10-14% w/v PEG 6000, 10% glycerol, and 4% tert-butanol, crystals grow within 1 to 14 days at 19°C, X-ray diffraction structure determination and analysis at 3.3 A resolution

Oryctolagus cuniculus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Oryctolagus cuniculus	16020	-
sarcoplasmic reticulum	-	Oryctolagus cuniculus	16529	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	-	Oryctolagus cuniculus
Mg2+	-	Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + Ca2+/cis	Oryctolagus cuniculus	the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity	ADP + phosphate + Ca2+/trans	-	?

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	P04191	isozyme 1a	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant biotinylated SERCA1a from Saccharomyces cerevisiae cells by solubilization with dodecylmaltoside, avidin affinity chromatography and gel filtration, to homogeneity, the biotin tag is cleaved off by thrombin	Oryctolagus cuniculus

Renatured (Commentary)

Renatured (Comment)	Organism
reconstitution of purified enzyme into proteoliposomes using 1,2-dioleoyl-sn-glycero-3-phosphocholine in a cholate buffer containing 30 mM Tris, pH 7.0, 0.4 M NaCl, 0.4 M sucrose, 1 mM MgCl2, 1 mM NaN3, 1% w/v sodium cholate, and 50 mM DTT, the enzyme shows nearly full activity	Oryctolagus cuniculus

Source Tissue

Source Tissue	Comment	Organism	Textmining
skeletal muscle	-	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + Ca2+/cis	the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity	Oryctolagus cuniculus	ADP + phosphate + Ca2+/trans	-	?

Synonyms

Synonyms	Comment	Organism
Ca2+-ATPase	-	Oryctolagus cuniculus
calcium-dependent ATPase	-	Oryctolagus cuniculus
sarcoplasmic-endoplasmic reticulum Ca2+-ATPase	-	Oryctolagus cuniculus
SERCA1a	-	Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Oryctolagus cuniculus