A conformational transition of the sarcoplasmic reticulum calcium transport ATPase induced by vanadate.
Vanadate binding to sarcoplasmic reticulum vesicles results in the loss of the externally located high affinity calcium binding sites of the calcium transport ATPase. Conversely the occupation by calcium of the internally located low affinity sites in the vanadate enzyme complex leads to the release of vanadate. Since the total number of calcium binding sites is not diminished by vanadate binding but slightly increases we conclude that vanadate binding induces a transition of the enzymes external high to internal low affinity calcium binding sites. The transposition of external to internal calcium binding sites is accompanied by a definite change in the structure of the sarcoplasmic reticulum membranes. On vanadate binding the asymmetrically arranged electron dense protein particles become symmetrically distributed.
D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D000001:Calcimycin / Q000494:pharmacology; D002118:Calcium / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D008854:Microscopy, Electron; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000187:drug effects* / Q000201:enzymology / Q000648:ultrastructure; D014638:Vanadates; D014639:Vanadium / Q000378:metabolism*
D014639:Vanadium; D000001:Calcimycin; D014638:Vanadates; D000252:Calcium-Transporting ATPases; D002118:Calcium