Literature summary for 7.2.2.10 extracted from

Stokes, D.L.; Pomfret, A.J.; Rice, W.J.; Glaves, J.P.; Young, H.S.
Interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals (2006), Biophys. J., 90, 4213-4223.

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme in complex with purified recombinant phospholamban, from 20 mM imidazole, pH 7.4, 100 mM KCl, 35 mM MgCl2, 0.5 mM EGTA, 0.25 mM Na3VO4, 0.03 mM thapsigargin, three freeze-thaw cycles using liquid nitrogen and thawing in hand, reconstitution at 4°C for several days to 1 week, analysis of interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals, overview	Oryctolagus cuniculus

Crystallization (Comment)

Organism

purified enzyme in complex with purified recombinant phospholamban, from 20 mM imidazole, pH 7.4, 100 mM KCl, 35 mM MgCl2, 0.5 mM EGTA, 0.25 mM Na3VO4, 0.03 mM thapsigargin, three freeze-thaw cycles using liquid nitrogen and thawing in hand, reconstitution at 4°C for several days to 1 week, analysis of interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals, overview

Oryctolagus cuniculus

Inhibitors

Inhibitors	Comment	Organism	Structure
phospholamban	phospholamban inhibits the enzyme by reducing the Ca2+ affinity, phospholamban mutant I40A is highly inhibitory, increases the dissociation constant of the enzyme for Ca2+	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+	binding structure and kinetics in the crystallized enzyme-phospholamban complex, overview	Oryctolagus cuniculus
Mg2+	binding structure in the crystallized enzyme-phospholamban complex, overview	Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Oryctolagus cuniculus	interaction of Ca2+-ATPase with phospholamban is involved in regulation of heart contractility, overview	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	P04191	-	-

Purification (Commentary)

Purification (Comment)	Organism
native enzyme from sekeletal muscle sarcoplasmic reticulum membranes by adsorption chromatography	Oryctolagus cuniculus

Renatured (Commentary)

Renatured (Comment)	Organism
reconstitution of purified enzyme with phospholamban in proteoliposomes, overview	Oryctolagus cuniculus

Source Tissue

Source Tissue	Comment	Organism	Textmining
skeletal muscle	from hind leg	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	interaction of Ca2+-ATPase with phospholamban is involved in regulation of heart contractility, overview	Oryctolagus cuniculus	?	-	?
additional information	interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals, overview	Oryctolagus cuniculus	?	-	?

Subunits

Subunits	Comment	Organism
More	interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals, overview	Oryctolagus cuniculus

Synonyms

Synonyms	Comment	Organism
SR Ca2+-ATPase	-	Oryctolagus cuniculus